[ { "id": "https://authors.library.caltech.edu/records/vef9g-7h248", "eprint_id": 106222, "eprint_status": "archive", "datestamp": "2023-08-19 02:14:28", "lastmod": "2023-10-20 23:13:36", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } }, { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } } ] }, "title": "Molecular Models of Amino Acids, Peptides, and Proteins", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1953 American Institute of Physics. \n\n(Received August 25, 1952) \n\nAided by a grant from the National Foundation for Infantile Paralysis. \n\nThe development of the molecular models described in this paper has been a collaborative effort in which many members of the staff of the California Institute of Technology have participated. We are especially grateful to Roger Hayward and William W. Schuelke for their ingenious solutions of many of the problems of design and construction, to Delmer D. Dill for his excellent workmanship, and to many members of the Institute faculty for their criticisms and suggestions. \n\nFor five years this work was aided by a grant from the National Foundation for Infantile Paralysis; more recently it has been aided by a grant from the National\nInstitutes of Health, U. S. Public Health Service.\n\n
Published - 1.1770803.pdf
", "abstract": "A set of accurate scale models has been developed for use in studies of the structures of amino acids, peptides, and proteins. Models representing atoms or groups of atoms built from hard wood to the scale 1 in.=1A are connected by a clamping device which maintains desired molecular configurations. These accurate models have been used as substitutes for calculation in investigations of the probable configuration of the polypeptide chain in proteins. Analogous models constructed of rubber\u2010like plastic to the scale 1 in.=2A and connected by snap fasteners are designed for qualitative studies of protein structure.", "date": "1953-08", "date_type": "published", "publication": "Review of Scientific Instruments", "volume": "24", "number": "8", "publisher": "American Institute of Physics", "pagerange": "621-627", "id_number": "CaltechAUTHORS:20201022-105318967", "issn": "0034-6748", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20201022-105318967", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "National Foundation for Infantile Paralysis" }, { "agency": "NIH" } ] }, "collection": "CaltechAUTHORS", "other_numbering_system": { "items": [ { "id": "1731", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1063/1.1770803", "primary_object": { "basename": "1.1770803.pdf", "url": "https://authors.library.caltech.edu/records/vef9g-7h248/files/1.1770803.pdf" }, "resource_type": "article", "pub_year": "1953", "author_list": "Corey, Robert B. and Pauling, Linus" }, { "id": "https://authors.library.caltech.edu/records/bzk7g-7ea04", "eprint_id": 62887, "eprint_status": "archive", "datestamp": "2023-08-19 02:11:02", "lastmod": "2023-10-25 21:57:34", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "L." } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "R. B." } } ] }, "title": "Stable Configurations of Polypeptide Chains", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1953 The Royal Society.", "abstract": "Several configurations of polypeptide chains involving planar amide groups with the\ndimensions found by experiment for simple substances, and hydrogen bonds between the\nNH groups and the carbonyl oxygen atoms, have been discovered. One of these structures,\nthe \u03b1-helix, with about 3\u00b77 amino-acid residues per turn of the helix, has been assigned to\nsynthetic polypeptides and proteins that give X-ray diagrams of the \u03b1-keratin type. The\nevidence supporting this assignment is reviewed. Other configurations of polypeptide chains,\nincluding the \u03b3-helix, three pleated-sheet structures, and the three-chain helical structure\nproposed for collagen, are described, and evidence bearing on their possible presence in\nproteins is discussed.", "date": "1953-03-11", "date_type": "published", "publication": "Proceedings of the Royal Society of London. Series B, Biological Sciences", "volume": "141", "number": "902", "publisher": "Royal Society", "pagerange": "21-33", "id_number": "CaltechAUTHORS:20151214-132412619", "issn": "0962-8452", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20151214-132412619", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechAUTHORS", "doi": "10.1098/rspb.1953.0012", "resource_type": "article", "pub_year": "1953", "author_list": "Pauling, L. and Corey, R. B." }, { "id": "https://authors.library.caltech.edu/records/ap0dn-dmt90", "eprint_id": 88255, "eprint_status": "archive", "datestamp": "2023-08-19 02:03:42", "lastmod": "2023-10-18 21:54:56", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The planarity of the amide group in polypeptides", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1952 American Chemical Society. \n\nReceived July 7, 1952.", "abstract": "[no abstract]", "date": "1952-08-06", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "74", "number": "15", "publisher": "American Chemical Society", "pagerange": "3964", "id_number": "CaltechAUTHORS:20180725-111210395", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180725-111210395", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "doi": "10.1021/ja01135a531", "resource_type": "article", "pub_year": "1952", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/cvxer-0k416", "eprint_id": 4602, "eprint_status": "archive", "datestamp": "2023-08-21 22:26:08", "lastmod": "2023-10-16 17:50:24", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "Configurations of polypeptide chains with equivalent cis amide group", "ispublished": "pub", "full_text_status": "public", "note": "Copyright \u00a9 1952 by the National Academy of Sciences \n\nCommunicated November 29, 1951 \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The National Institutes of Health, Public Health Service. \n\nContribution No. 1646 from the Gates and Crellin Laboratories of Chemistry, Californmia Institute of Technology, Pasadena", "abstract": "In recent papers [1-3] we have pointed out that stable configurations of polypeptide chains must show the bond distances and bond angles found in simple peptides and related simple substances, that each amide group must be planar, with either the cis-configuration or the trans-configuration about the C'-N bond, and that the carbonyl and imino groups (except for proline or hydroxyproline residues) must be involved in the formation of hydrogen bonds, with N-H\u2022\u2022\u2022O distance approximately 2.8 \u00c5, and with the oxygen atom nearly on the N-H axis. We have also presented evidence indicating that certain configurations around the two single bonds from the amide groups to the a carbon atom are energetically favored, and have discussed the 36 polypeptide-chain structures involving equivalent trans-amide groups with one or another of six favored azimuthal orientations about the N-C single bond and also one of six favored orientations about the C-C' single bond. [4] In the present paper we discuss the 36 configurations of equivalent cis-amide groups corresponding to these favored orientations, and also a few other configurations of cis-amide groups.", "date": "1952-02-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "38", "number": "2", "publisher": "National Academy of Sciences", "pagerange": "86-93", "id_number": "CaltechAUTHORS:PAUpnas52b", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas52b", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas52b.pdf", "url": "https://authors.library.caltech.edu/records/cvxer-0k416/files/PAUpnas52b.pdf" }, "resource_type": "article", "pub_year": "1952", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/hq2fj-hqw64", "eprint_id": 7777, "eprint_status": "archive", "datestamp": "2023-08-21 22:24:58", "lastmod": "2023-10-16 21:05:35", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated September 4, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The National Institutes of Health, Public Health Service.", "abstract": "In recent papers we have described several configurations of polypeptide chains with interatomic distances, bond angles, and other structural features as indicated by the studies in these Laboratories of the structure of crystals of amino acids, simple peptides, and related substances, and have presented evidence for their presence in synthetic polypeptides, fibrous proteins, and globular proteins.(1-9)", "date": "1951-11-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "11", "publisher": "National Academy of Sciences", "pagerange": "729-740", "id_number": "CaltechAUTHORS:PAUpnas51a", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51a", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "doi": "10.1073/pnas.37.11.729", "primary_object": { "basename": "PAUpnas51a.pdf", "url": "https://authors.library.caltech.edu/records/hq2fj-hqw64/files/PAUpnas51a.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/62dzp-eys45", "eprint_id": 50378, "eprint_status": "archive", "datestamp": "2023-08-19 01:50:57", "lastmod": "2023-10-17 23:24:59", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "X-Ray Crystallographic Studies of Compounds of Biological Interest", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1951 Annual Reviews.", "abstract": "In her review of the years 1944 to 1947, Dr. Crowfoot (1) commented upon the progress which had been made in our knowledge of organic structures since the first of the Annual Review series (1936) by Sponsler & Dore and called attention to the increasing productivity in recent years which has resulted from the growing power of x-ray analytical methods. This accelerated output of structure determinations has continued during the years 1948 to 1950. The first issue of Acta Crystallographica appeared in 1948,\nand already more than 60 articles dealing with the crystal structures of organic compounds have been published in its pages alone. But the increased number of structure determinations is probably less significant than the greatly increased accuracy with which they can now be made. This increased accuracy may be largely attributed to improved computational techniques for refining atomic coordinates by the calculation of Fourier series or by the\nmethod of least squares (2).", "date": "1951-07", "date_type": "published", "publication": "Annual Review of Biochemistry", "volume": "20", "number": "1", "publisher": "Annual Reviews", "pagerange": "131-148", "id_number": "CaltechAUTHORS:20141014-134311828", "issn": "0066-4154", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20141014-134311828", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechAUTHORS", "other_numbering_system": { "items": [ { "id": "1492", "name": "Caltech Gates and Crellin Laboratory of Chemistry" } ] }, "doi": "10.1146/annurev.bi.20.070151.001023", "resource_type": "article", "pub_year": "1951", "author_list": "Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/a6880-hst35", "eprint_id": 10215, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:28", "lastmod": "2023-10-16 22:44:28", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "Atomic coordinates and structure factors for two helical configurations of polypeptide chains", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The United States Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1550.", "abstract": "During recent years we have been gathering information about interatomic distances, bond angles, and other properties of simple substances related to proteins, and have been attempting to formulate configurations of the polypeptide chain that are compatible with this information and that might constitute a structural feature of proteins. We have reported the discovery of two helical configurations that satisfy these conditions. (1,2) In the following paragraphs we discuss the atomic positions for these configurations, and their form factors for diffraction of x-rays in the equatorial direction.", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "235-240", "id_number": "CaltechAUTHORS:PAUpnas51g", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51g", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51g.pdf", "url": "https://authors.library.caltech.edu/records/a6880-hst35/files/PAUpnas51g.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/esvfg-ahe09", "eprint_id": 8084, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:18", "lastmod": "2023-10-16 21:08:32", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The pleated sheet, a new layer configuration of polypeptide chains", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The United States Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1552.", "abstract": "For many years it has been assumed that in silk fibroin, stretched hair and muscle, and other proteins with the \u03b2-keratin structure the polypeptide chains are extended to nearly their maximum length, about 3.6 A per residue, and during the last decade it has been assumed also that the chains form lateral hydrogen bonds with adjacent chains, which have the opposite orientation. A hydrogen-bonded layer of this sort is represented diagrammatically in figure 1.(1-4)", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "251-256", "id_number": "CaltechAUTHORS:PAUpnas51e", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51e", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51e.pdf", "url": "https://authors.library.caltech.edu/records/esvfg-ahe09/files/PAUpnas51e.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/jbm9b-92736", "eprint_id": 8082, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:09", "lastmod": "2023-10-16 21:08:28", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The polypeptide-chain configuration in hemoglobin and other globular proteins", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The United States Public Health Service. We acknowledge with gratitude the assistance and encouragement of our colleagues in The Gates and Crellin Laboratories of Chemistry throughout the period during which the studies reported in this series of papers and also the investigations on which this work is based were made. We are especially grateful to Professor Verner Schomaker, who has helped by giving us the benefit of both his deep understanding of structural chemistry and his profound critical insight. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1556.", "abstract": "In the immediately preceding papers we have described several hydrogen-bonded planar-amide configurations of polypeptide chains, and have discussed the evidence bearing on the question of their presence in fibrous proteins. It seems worth while to consider the possibility that these configurations - the pleated sheet, the 3.7-residue \u03b1 helix, the 5.1-residue \u03b3 helix, and the three-chain collagen helix-are represented in molecules of the globular proteins.", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "282-285", "id_number": "CaltechAUTHORS:PAUpnas51c", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51c", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51c.pdf", "url": "https://authors.library.caltech.edu/records/jbm9b-92736/files/PAUpnas51c.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/sj5w2-j1v47", "eprint_id": 9674, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:23", "lastmod": "2023-10-16 22:25:22", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The structure of fibrous proteins of the collagen-gelatin group", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis work was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The U.S. Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1555.", "abstract": "Collagen is a very interesting protein. It has well-defined mechanical properties (great strength, reversible extensibility through only a small range) that make it suited to the special purposes to which it is put in the animal body, as in tendon, bone, tusk, skin, the cornea of the eye, intestinal tissue, and probably rather extensively in reticular structures of cells. During the last thirty years, following the pioneer work of Herzog and Jancke,(1) a number of investigators have attempted to find the structure of collagen (and of gelatin, which gives similar x-ray photographs), but no one has previously proposed any precisely described configuration, nor has attempted to account for the positions and intensities of the x-ray diffraction maxima.", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "272-281", "id_number": "CaltechAUTHORS:PAUpnas51f", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51f", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51f.pdf", "url": "https://authors.library.caltech.edu/records/sj5w2-j1v47/files/PAUpnas51f.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/hm68k-2he24", "eprint_id": 8083, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:13", "lastmod": "2023-10-16 21:08:30", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The structure of hair, muscle, and related proteins", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The United States Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1554.", "abstract": "It is thirty years since x-ray photographs were first made of hair, muscle, nerve, and sinew, by Herzog and Jancke.(1) During this period, despite the efforts of many investigators, the photographs have eluded detailed interpretation, and the molecular structures of the proteins have remained undetermined. In the present paper we propose structures for hair, muscle, and related proteins in the extended state (\u03b2 keratin and \u03b2 myosin) and the contracted state (\u03b1 keratin and \u03b1 myosin), and discuss the extent to which the diffraction data are accounted for by the proposed structures.", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "261-271", "id_number": "CaltechAUTHORS:PAUpnas51d", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51d", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51d.pdf", "url": "https://authors.library.caltech.edu/records/hm68k-2he24/files/PAUpnas51d.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/36szn-k1w78", "eprint_id": 8081, "eprint_status": "archive", "datestamp": "2023-08-21 22:22:04", "lastmod": "2023-10-16 21:08:26", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The structure of synthetic polypeptides", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated March 31, 1951. \n\nThis investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The U.S. Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1551.", "abstract": "In a preliminary communication last year(1) we stated that there are only two helical configurations of polypeptide chains in which the residues are all equivalent and intramolecular hydrogen bonds are formed, and in which the interatomic distances, bond angles, and other structural features, especially the coplanarity of the conjugated amide system, are as required by earlier work in these Laboratories on amino acids, simple peptides, and other substances related to protein's. These two helical configurations were described in detail in a later paper(2) and it was mentioned that there is evidence that they occur in \u03b1 keratin, \u03b1 myosin, supercontracted keratin and myosin, and other fibrous proteins, and also constitute an important structural feature of hemoglobin and other globular proteins.(3) In the following paragraphs we discuss evidence that one of the helical structures is assumed also by synthetic polypeptides.", "date": "1951-05-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "5", "publisher": "National Academy of Sciences", "pagerange": "241-250", "id_number": "CaltechAUTHORS:PAUpnas51b", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51b", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51b.pdf", "url": "https://authors.library.caltech.edu/records/36szn-k1w78/files/PAUpnas51b.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/v4zz4-cqd29", "eprint_id": 6990, "eprint_status": "archive", "datestamp": "2023-08-21 22:21:49", "lastmod": "2023-10-16 20:39:03", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } }, { "id": "Branson-H-R", "name": { "family": "Branson", "given": "H. R." } } ] }, "title": "The Structure of Proteins: Two Hydrogen-Bonded Helical Configurations of the Polypeptide Chain", "ispublished": "pub", "full_text_status": "public", "note": "Copyright \u00a9 1951 by the National Academy of Sciences \n\nCommunicated February 28, 1951 \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1538.", "abstract": "During the past fifteen years we have been attacking the problem of the structure of proteins in several ways. One of these ways is the complete and accurate determination of the crystal structure of amino acids, peptides, and other simple substances related to proteins, in order that information about interatomic distances, bond angles, and other configurational parameters might be obtained that would permit the reliable prediction of reasonable configurations for the polypeptide chain. We have now used this information to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; we think that it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of synthetic polypeptides. A letter announcing their discovery was published last year [1]. \n\nThe problem that we have set ourselves is that of finding all hydrogen-bonded structures for a single polypeptide chain, in which the residues are equivalent (except for the differences in the side chain R). An amino acid residue (other than glycine) has no symmetry elements. The general operation of conversion of one residue of a single chain into a second residue equivalent to the first is accordingly a rotation about an axis accompanied by translation along the axis. Hence the only configurations for a chain compatible with our postulate of equivalence of the residues are helical configurations. For rotational angle 180\u00b0 the helical configurations may degenerate to a simple chain with all of the principal atoms, C, C' (the carbonyl carbon), N, and O, in the same plane.", "date": "1951-04-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "4", "publisher": "National Academy of Sciences", "pagerange": "205-211", "id_number": "CaltechAUTHORS:PAUpnas51h", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51h", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "PAUpnas51h.pdf", "url": "https://authors.library.caltech.edu/records/v4zz4-cqd29/files/PAUpnas51h.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Pauling, Linus; Corey, Robert B.; et el." }, { "id": "https://authors.library.caltech.edu/records/mgf06-7xp66", "eprint_id": 76540, "eprint_status": "archive", "datestamp": "2023-08-19 01:44:28", "lastmod": "2023-10-25 16:05:54", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "Two hydrogen-bonded spiral configurations of the polypeptide chain", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1950 American Chemical Society. \n\nReceived October 16, 1950. \n\nWe are indebted to Drs. H. R. Branson and S. Weinbaum for assistance. Our work has been aided by grants from the Rockefeller Foundation and the National Foundation for Infantile Paralysis. A detailed account of the work will be published soon.", "abstract": "During the past fifteen years we have been carrying on a program of determination of the detailed atomic arrangements of crystals of amino acids, peptides, and other simple substances related to proteins, in order to obtain structural information that would permit the precise prediction of reasonable configurations of proteins. We have now used this information to construct two hydrogen-bonded spiral configurations of the polypeptide chain, with the residues all equivalent, except for variation in the side chain.", "date": "1950-11", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "72", "number": "11", "publisher": "American Chemical Society", "pagerange": "5349-5349", "id_number": "CaltechAUTHORS:20170412-163237901", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20170412-163237901", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Rockefeller Foundation" }, { "agency": "National Foundation for Infantile Paralysis" } ] }, "other_numbering_system": { "items": [ { "id": "1481", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01167a545", "resource_type": "article", "pub_year": "1950", "author_list": "Pauling, Linus and Corey, Robert B." }, { "id": "https://authors.library.caltech.edu/records/6ttkj-abw16", "eprint_id": 88262, "eprint_status": "archive", "datestamp": "2023-08-19 01:39:47", "lastmod": "2023-10-18 21:55:24", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Shoemaker-D-P", "name": { "family": "Shoemaker", "given": "David P." } }, { "id": "Donohue-J", "name": { "family": "Donohue", "given": "Jerry" } }, { "id": "Schomaker-V", "name": { "family": "Schomaker", "given": "Verner" } }, { "id": "Corey-R-B", "name": { "family": "Corey", "given": "Robert B." } } ] }, "title": "The Crystal Structure of L_s-Threonine", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1950 American Chemical Society. \n\nReceived September 12, 1949. \n\nAided by a grant from the National Foundation for Infantile Paralysis, Inc. \n\nNational Research Council Predoctoral Fellow, 1946-1947. Part of the work described here was included in a dissertation submitted by D. P. Shoemaker to the California Institute of Technology in partial fulfillment of the requirements for the Degree of Doctor of Philosophy. \n\nMost of the computational work was done by Miss Lillian Casler and Mrs. Jean Smith, and the figures were prepared by Mrs. Maryellin Reinecke. The authors are grateful to Professor Linus Pauling for his interest, encouragement, and helpful criticism. They wish to express their thanks to Professor Werner Nowacki of Bern, Switzerland, who assisted in the work with the structure factor maps and participated in the computation of the two-dimensional Fourier syntheses and of a second Patterson function. Grateful acknowledgment is also expressed for the financial support of the National Foundation for Infantile Paralysis, Inc.", "abstract": "In the three-year investigation described below, we have determined by X-ray diffraction methods the crystal structure of L-threonine. This work has confirmed the molecular structure and the relative configurations of the asymmetric centers as deduced by Rose and co-workers, and has also given detailed information concerning bond lengths, bond angles, hydrogen bonding, and van der Waals packing. Because of our high confidence in the experimental data, we have striven toward the fullest possible utilization of their precision. In this connection we have developed, improved, or used for the first time a number of new techniques: the use of the entire three-dimensional Patterson function, a more rapidly convergent non-centrosymmetric Fourier method, an analytical method for locating Fourier maxima, a \"three-dimensional\" least squares procedure for the simultaneous refinement of all positional parameters (except those of hydrogen atoms), punched card methods for calculating structure factors and for least squares refinement, and methods for estimating the precision of the parameter determination. Most of these will be described only briefly here, and some will be described in detail elsewhere.", "date": "1950-06", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "72", "number": "6", "publisher": "American Chemical Society", "pagerange": "2328-2349", "id_number": "CaltechAUTHORS:20180725-111210982", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180725-111210982", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "National Foundation for Infantile Paralysis" }, { "agency": "National Research Council" } ] }, "collection": "CaltechAUTHORS", "other_numbering_system": { "items": [ { "id": "1331", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01162a002", "resource_type": "article", "pub_year": "1950", "author_list": "Shoemaker, David P.; Donohue, Jerry; et el." } ]