Abstract
The properties of proteins are determined not only by the sequence of amino-acid residues in the polypeptide chains, but also by the configuration of the chains—the way in which the chains are coiled or folded. It is probable that denaturation, the loss of some of the specific properties of a native protein, may in many cases be the result simply of a change in configuration of the polypeptide chains, without any change whatever in the sequence of amino-acid residues.
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References
Albrecht, G. and R. B. Corey: The Crystal Structure of Glycine. J. Amer. Chem. Soc. 61, 1087 (1939).
Ambrose, E. J. and A. Elliott: The Structure of Synthetic Polypeptides. II. Investigation with Polarized Infra-red Spectroscopy. Proc. Roy. Soc. (London), Ser. A 205, 47 (1951).
Ambrose, E. J. and W. E. Hanby: Evidence of Chain Folding in a Synthetic Polypeptide and in Keratin. Nature (London) 163, 483 (1949).
Arndt, U. W. and D. P. Riley: Intra-helix S—S Linked Structures for Insulin. Nature (London) 172, 245 (1953).
Astbury, W. T. (leader of the discussion): A Discussion on the Structure of Proteins. Proc. Roy. Soc. (London), Ser. B 141, 1 (1953).
Astbury, W. T. and A. Street: X-ray Studies of the Structure of Hair, Wool, and Related Fibres. I. General. Philos. Trans. Roy. Soc. (London), Ser. A 230, 75 (1931).
Astbury, W. T. and C. Weibull: X-ray Diffraction Study of the Structure of Bacterial Flagella. Nature (London) 163, 280 (1949).
Astbury, W. T. and H. J. Woods: X-ray Studies of the Structure of Hair, Wool, and Related Fibres. II. The Molecular Structure and Elastic Properties of Hair Keratin. Philos. Trans. Roy. Soc. (London), Ser. A 232, 333 (1933).
Badger, R. M. and H. Rubalcava: The Infrared Absorption Spectra of Amides in Solution and Their Relation to the Spectra of Polypeptides. Proc. Nat. Acad. Sci. (U.S.A.) 40, 12 (1954).
Bailey, K., W. T. Astbury and K. M. Rudall: Fibrinogen and Fibrin as Members of the Keratin-Myosin Group. Nature (London) 151, 716 (1943).
Bamford, C. H., L. Brown, A. Elliott, W. E. Hanby and I. F. Trotter: Structure of Synthetic Polypeptides. Nature (London) 169, 357 (1952).
Bamford, C. H., L. Brown, A. Elliott, W. E. Hanby and I. F. Trotter: Some New Investigations on the Structure of Synthetic Polypeptides. Proc. Roy. Soc. (London), Ser. B 141, 49 (1953).
Bamford, C. H., L. Brown, A. Elliott, W. E. Hanby and I. F. Trotter: Alpha-und Beta-Forms of Poly-L-Alanine. Nature (London) 173. 27 (1954).
Bamford, C. H., W. E. Hanby and F. Happey: The Structure of Synthetic Polypeptides. I. X-ray Investigation. Proc. Roy. Soc. (London), Ser. A 205, 30 (1951).
Bear, R. S.: Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
Bernal, J. D.: The Crystal Structure of the Natural Amino Acids and Related Compounds. Z. Kristallogr., Mineral., Petrogr. 78, 363 (1931).
Bernal, J. D. and D. Crowfoot: X-ray Photographs of Crystalline Pepsin. Nature (London) 133, 794 (1934).
Bijvoet, J. M., A. F. Peerdeman and A. J. van Bommel: Determination of the Absolute Configuration of Optically Active Compounds by Means of X-rays. Nature (London) 168, 271 (1951).
Blum, J. and D. R. Davies: The Crystal Structure of Parabanic Acid (unpublished).
Boehm, G. und H. H. Weber: Das Röntgendiagramm von gedehnten Myosinfäden. Kolloid-Z. 61, 269 (1932).
Boyes-Watson, J., E. Davidson and M. F. Perutz: An X-ray Study of Horse Methaemoglobin. I. Proc. Roy. Soc. (London), Ser. A 191, 83 (1947).
Bragg, L.: X-ray Analysis of the Haemoglobin Molecule. Proc. Roy. Soc. (London), Ser. B 141, 67 (1953).
— Application of X-ray Optics to Proteins. Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
Bragg, L., J. C. Kendrew and M. F. Perutz: Polypeptide Chain Configurations in Crystalline Proteins. Proc. Roy. Soc. (London), Ser. A 203, 321 (1950).
Bragg, L. and M. F. Perutz: The Structure of Haemoglobin. Proc. Roy. Soc. (London), Ser. A 213, 425 (1952).
Brill, R.: Über Scidenfibroin. I. Liebigs Ann. Chem. 434, 204 (1923).
Carpenter, G. B. and J. Donohue: The Crystal Structure of N-Acetylglycine. J. Amer. Chem. Soc. 72, 2315 (1950).
Cochran, W., F. H. C. Crick and V. Vand: The Structure of Synthetic Polypeptides. I. The Transform of Atoms on a Helix. Acta Crystallogr. 5, 581 (1952).
Cochran, W. and B. R. Penfold: The Crystal Structure of L-Glutamine. Acta Crystallogr. 5, 644 (1952).
Cohen, C. and R. S. Bear: Helical Polypeptide Chain Configuration in Collagen. J. Amer. Chem. Soc. 75, 2783 (1953).
Corey, R. B.: The Crystal Structure of Diketopiperazine. J. Amer. Chem. Soc. 60, 1598 (1938).
Corey, R. B.: X-ray Diffraction Studies of Crystalline Amino Acids and Peptides. Fortschr. Chem. organ. Naturstoffe 8, 310 (1951).
Corey, R. B. and J. Donohue: Interatomic Distances and Bond Angles in the Polypeptide Chain of Proteins. J. Amer. Chem. Soc. 72, 2899 (1950).
Corey, R. B. and L. Pauling: Fundamental Dimensions of Polypeptide Chains. Proc. Roy. Soc. (London), Ser. B 141, 10 (1953).
Crick, F. H. C: Is α-Keratin a Coiled Coil? Nature (London) 170, 882 (1952).
Crick, F. H. C: The Height of the Vector Rods in the Three-dimensional Patterson of Haemoglobin. Acta Crystallogr. 5, 381 (1952).
Crick, F. H. C.: The Strength of the 10-Å. Reflexions in Haemoglobin. Acta Crystallogr. 6, 600 (1953).
Crick, F. H. C: Fourier Transform of a Coiled Coil. Acta Crystallogr. 6, 685 (1953).
Crick, F. H. C: The Packing of α-Helices: Simple Coiled Coils. Acta Crystallogr. 6, 689 (1953).
Crowfoot, D., C. W. Bunn, B. W. Rogers-Low and A. Turner-Jones: The X-ray Crystallographic Investigation of the Structure of Penicillin. Chap. 11. The Chemistry of Penicillin. (Ed., H. T. Clarke, J. R. Johnson and R. Robinson) Princeton: Univ. Press. 1949.
Dawson, B.: The Crystal Structure of DL-Glutamic Acid Hydrochloride. Acta Crystallogr. 6, 81 (1953).
Derksen, J. C. and G. C. Heringa: Szymonowicz-Festschr., Polska Gaz. Lekarska 15, 532 (1936).
Donohue, J.: The Crystal Structure of DL-Alanine. II. Revision of Parameters by Three-dimensional Fourier Analysis. J. Amer. Chem. Soc. 72, 949 (1950).
Donohue, J.: The Hydrogen Bond in Organic Crystals. J. Physic. Chem. 56, 502 (1952).
Donohue, J.: Hydrogen Bonded Helical Configurations of the Polypeptide Chains. Proc. Nat. Acad. Sci. (U. S.A.) 39, 470 (1953).
Donohue, J. and K. N. Trueblood: The Crystal Structure of Hydroxy-L-Proline. I. Interpretation of the Three-dimensional Patterson function. Acta Crystallogr. 5, 414 (1952).
Donohue, J. and K. N. Trueblood: The Crystal Structure of Hydroxy-L-Proline. II. Determination and Description of the Structure. Acta Crystallogr. 5, 419 (1952).
Dyer, H. B.: The Crystal Structure of Cysteyl-glycine Sodium Iodide. Acta Crystallogr. 4, 42 (1951).
Herzog, R. O. und W. Jancke: Über den physikalischen Aufbau einiger hochmolekularer organischer Verbindungen. 1. vorl. Mitt. Ber. dtsch. chem. Ges. 53, 2162 (1920); Festschrift der Kaiser Wilhelm-Ges., S. 118 (1921).
Huggins, M. L.: Hydrogen Bridges in Organic Compounds. J. Organ. Chem. (U. S. A.) 1, 407 (1936).
Huggins, M. L.: The Structure of Fibrous Proteins. Chem. Rev. 32, 195 (1943).
Hughes, E. W., A. B. Biswas and J. N. Wilson: The Crystal Structure of α-Glycylglycine. Acta Crystallogr. (to be published).
Hughes, E. W. and W. J. Moore: The Crystal Structure of β-Glycylglycine. J. Amer. Chem. Soc. 71, 2618 (1949).
Katz, L., R. A. Pasternak and R. B. Corey: Configuration of the Peptide Link and of Asparagine in Glycyl-L-Asparagine. Nature (London) 170, 1066 (1952).
Kendrew, J. C.: Structure of Proteins. Nature (London) 173, 57 (1954).
Kratky, O.: Über Scidenfibroin. II. Z. physik. Chem., Abt. B 5, 297 (1929).
Kratky, O. und S. Kuriyama: Über Scidenfibroin. III. Z. physik. Chem., Abt. B 11, 363 (1930).
Kratky, O. und H. Mark: Anwendung physikalischer Methoden zur Erforschung von Naturstoffen: Form und Größe dispergierter Moleküle. Röntgenographie. Fortschr. Chem. organ. Naturstoffe 1, 255 (1938).
Leonard, J. E. and R. A. Pasternak: The Unit-cell Dimensions and the Space Groups of Some Simple Peptides of Glycine, Alanine, and Leucine. Acta Crystallogr. 5, 150 (1952).
Lévy, H. A. and R. B. Corey: The Crystal Structure of DL-Alanine. J. Amer. Chem. Soc. 63, 2095 (1941).
Lonsdale, K.: Divergent-beam X-ray Photography of Crystals. Trans. Roy. Soc. (London), Ser. A 240, 244 (1947).
Low, B. W.: In: The Proteins, Vol. 1, chapter 4, p. 235. (Ed., H. Neurath and K. Bailey) New York: Acad. Press. 1953.
Low, B. W. and R. B. Baybutt: The Pi Helix—A Hydrogen Bonded Configuration of the Polypeptide Chain. J. Amer. Chem. Soc. 74, 5806 (1952).
Low, B. W. and H. J. Grenville-Wells: Generalized Mathematical Relationships for Polypeptide Chain Helices. The Coordinates of the π Helix. Proc. Nat. Acad. Sci. (U. S.A.) 39, 785 (1953).
MacArthur, I.: Structure of α-Keratin. Nature (London) 152, 38 (1943).
Marsh, R. E., L. Pauling and R. B. Corey: The Structure of Silk Fibroin (to be published).
Mathieson, A. McL.: The Crystal Structure of the Dimorphs of DL-Methionine. Acta Crystallogr. 5, 332 (1952).
Mathieson, A. McL.: Polymorphism of DL-Norleucine. Acta Crystallogr. 6, 399 (1953).
Meyer, K. H. und H. Mark: Über den Aufbau des Sciden-Fibroins. Ber. dtsch. chem. Ges. 61, 1932 (1928).
Mirsky, A. E. and L. Pauling: On the Structure of Native, Denatured, and Coagulated Proteins. Proc. Nat. Acad. Sci. (U. S. A.) 22, 439 (1936).
Mizushima, S., T. Simanouti, S. Nagakura, K. Kuratani, M. Tsuboi, H. Baba and O. Fujioka: The Molecular Structure of N-Methylacetamide. J. Amer. Chem. Soc. 72, 3490 (1950).
Neuberger, A.: Stereochemistry of Amino Acids. Adv. Protein Chem. 4, 297 (1948), especially p. 321.
Newman, R. and R. M. Badger: The Infrared Spectra of N-Acetylglycine and Diketopiperazine Polarized Radiation at 25° and at — 185° C. J. Chem. Physics 19, 1147 (1951).
Palmer, K. J.: Lysozyme Chloride. I. X-ray Diffraction Study of Lysozyme Chloride. Abstr. of Papers, 1st Intern. Union Crystallogr., p. 17 (1948); cf. Structure Reports for 1947–1948, 11, 729.
Pasternak, R. A.: Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
— The Crystal Structure of Glycyl-L-Tryptophan Dihydrate (unpublished).
Pasternak, R. A., L. Katz and R. B. Corey: The Crystal Structure of Glycyl-L-Asparagine. Acta Crystallogr. 7, 225 (1954).
Pasternak, R. A. and J. E. Leonard: The Unit-cell Dimensions and the Space Groups of Some Alanyl Peptides. Acta Crystallogr. 5, 152 (1952).
Pauling, L.: A Theory of the Structure and Process of Formation of Antibodies. J. Amer. Chem. Soc. 62, 2643 (1940).
Pauling, L.: Discussion, Colloques Intern. Centre Nat. Rech. Sci. XVIII. La liaison chimique. Paris, avril 1948, p. 155.
Pauling, L.: On the Stability of the S8 Molecule and the Structure of Fibrous Sulfur. Proc. Nat. Acad. Sci. (U. S.A.) 35, 495 (1949).
Pauling, L.: Les protéines. Rapports et discussions. 9e ConScil de Chimie, Inst. Intern. Chimie Solvay. (Ed., R. Stoops) Bruxelles. 1953, p. 63.
Pauling, L. and R. B. Corey: Two Hydrogen-bonded Spiral Configurations of the Polypeptide Chain. J. Amer. Chem. Soc. 72, 5349 (1950).
Pauling, L. and R. B. Corey: Atomic Coordinates and Structure Factors for Two Helical Configurations of Polypeptide Chains. Proc. Nat. Acad. Sci. (U. S. A.) 37, 235 (1951).
Pauling, L. and R. B. Corey: The Structure of Synthetic Polypeptides. Proc. Nat. Acad. Sci. (U. S.A.) 37, 241 (1951).
Pauling, L. and R. B. Corey: The Pleated Sheet; A New Layer Configuration of Polypeptide Chains. Proc. Nat. Acad. Sci. (U.S.A.) 37, 251 (1951).
Pauling, L. and R. B. Corey: The Structure of Hair, Muscle, and Related Proteins. Proc. Nat. Acad. Sci. (U. S. A.) 37, 261 (1951).
Pauling, L. and R. B. Corey: The Structure of Fibrous Proteins of the Collagen-Gelatin Group. Proc. Nat. Acad. Sci. (U. S. A.) 37, 272 (1951).
Pauling, L. and R. B. Corey: The Polypeptide-Chain Configuration in Hemoglobin and Other Globular Proteins. Proc. Nat. Acad. Sci. (U. S.A.) 37, 282 (1951).
Pauling, L. and R. B. Corey: Configurations of Polypeptide Chains with Favored Orientations Around Single Bonds: Two New Pleated Sheets. Proc. Nat. Acad. Sci. (U. S. A.) 37, 729 (1951).
Pauling, L. and R. B. Corey: Two Pleated Sheet Configurations of Polypeptide Chains Involving Both Cis and Trans Amide Groups. Proc. Nat. Acad. Sci. (U. S. A.) 39, 247 (1953).
Pauling, L. and R. B. Corey: Two Rippled Sheet Configurations of Polypeptide Chains, and a Note about the Pleated Sheets. Proc. Nat. Acad. Sci. (U. S. A.) 39, 253 (1953).
Pauling, L. and R. B. Corey: Stable Configurations of Polypeptide Chains. Proc. Roy. Soc. (London), Ser. B 141, 21 (1953).
Pauling, L. and R. B. Corey: Compound Helical Configurations of Polypeptide Chains: Structure of Proteins of the α Keratin type. Nature (London) 171, 59 (1953).
Pauling, L., R. B. Corey and H. R. Branson: The Structure of Proteins: Two Hydrogen-bonded Helical Configurations of the Polypeptide Chain. Proc. Nat. Acad. Sci. (U. S. A.) 37, 205 (1951).
Pauling, L., R. B. Corey and L. R. Lavine: (unpublished).
Perutz, M. F.: An X-ray Study of Horse Methaemoglobin. II. Proc. Roy. Soc. (London), Ser. A 195, 474 (1949).
Perutz, M. F.: Crystallography. Structure of Proteins and Related Compounds. Annu. Rep. Progr. Chem. 48, 361 (1951).
Perutz, M. F.: New X-ray Evidence on the Configuration of Polypeptide Chains. Nature (London) 167, 1053 (1951).
— A Fourier Projection of Hemoglobin. Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
Pitt, G. J.: A Refinement of the Crystal Structure of Potassium Benzyl-penicillin. Acta Crystallogr. 5, 770 (1952).
Randall, J. T.: Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
Riley, D. P.: Conference on the Structure of Proteins, Pasadena, Calif., Sept. 1953.
Riley, D. P. and U. W. Arndt: New Type of X-ray Evidence on the Molecular Structure of Globular Proteins. Nature (London) 169, 138 (1952).
Riley, D. P. and U. W. Arndt: X-ray Scattering by Some Native and Denatured Proteins in the Solid State. Proc. Roy. Soc. (London), Ser. B 141, 93 (1953).
Robinson, C. and E. J. Ambrose: Atomic Models. 2. The Use of Atomic Models in Investigating Stable Configurations of Protein Chains. Trans. Faraday Soc. 48, 854 (1952).
Romers, C.: The Structure of Oxamide. Acta Crystallogr. 6, 429 (1953).
Rudall, K. M.: Fibrous Proteins. Sympos. Soc. Dyers Colourists, England, 1946, p. 15.
Rudall, K. M.: The Proteins of the Mammalian Epidermis. Adv. Protein Chem. 7, 253 (1952).
Rudall, K. M.: Elastic Properties and α,β-Transformation of Fibrous Proteins. Proc. Roy. Soc. (London), Ser. B 141, 39 (1953).
Sanger, F. and E. O. P. Thompson: The Amino-acid Sequence in the Glycyl Chain of Insulin. 2. The Investigation of Peptides from Enzymic Hydrolysates. Biochemie. J. 53, 366 (1953).
Sanger, F. and H. Tuppy: The Amino-acid Sequence in the Phenylalanyl Chain of Insulin. 2. The Investigation of Peptides from Enzymic Hydrolysates. Biochemie. J. 49, 481 (1951).
Schuch, A. F., L. L. Merritt, Jr. and J. H. Sturdivant: The Crystal Structure of Urea Oxalate (unpublished).
Shoemaker, D. P., R. E. Barieau, J. Donohue and C. S. Lu: The Crystal Structure of DL-Serine. Acta Crystallogr. 6, 241 (1953).
Shoemaker, D. P., J. Donohue, V. Schomaker and R. B. Corey: The Crystal Structure of Ls-Threonine. J. Amer. Chem. Soc. 72, 2328 (1950).
Simanouti, T. and S. Mizushima: Intramolecular Rotation and the Structure of High Polymers. I. The Structure of Polypeptide Chain. Bull. Chem. Soc. Japan 21. 1 (1948).
Sly, W. G. and J. H. Sturdivant: The Crystal Structure of Oxamide (unpublished).
Smits, D. W. and E. H. Wiebenga: The Crystal Structure of Glycyl-L-Tyrosine Hydrochloride. Acta Crystallogr. 6, 531 (1953).
Tranter, T. C.: Unit-cell Dimensions and Space Groups of Synthetic Peptides. I. Glycyl-L-Tyrosine, Glycyl-L-Tyrosine Hydrochloride, Glycyl-DL-Serine, and Glycyl-DL-Leucine. Acta Crystallogr. 5, 843 (1952).
Tranter, T. C.: Unit-cell Dimensions and Space Groups of Synthetic Peptides. II. Glycyl-L-Alanine, Glycyl-L-Alanine Hydrochloride, Glycyl-L-Alanine Hydrobromide, and Glycyl-L-Tryptophane. Acta Crystallogr. 6, 805 (1953).
Tranter, T. C.: Unit-cell Dimensions and Space Groups of Synthetic Peptides. III. Glycyl-L-valine Hydrobromide, Glycyl-L-valine Hydrochloride, and DL-Alanyl-DL-methionine. Acta Crystallogr. 7, 134 (1954).
Tranter, T. C.: Crystal Structure of Glycyl-L-alanine Hydrobromide. Nature (London) 173, 221 (1954).
Trogus, C. und K. Hess: Zur Kenntnis der natürlichen Sciden und ihres Verhaltens gegen Säuren und Basen. Biochem. Z. 260, 376 (1933).
Vaughan, P. and J. Donohue: The Structure of Urea. Interatomic Distances and Resonance in Urea and Related Compounds. Acta Crystallogr. 5, 530 (1952).
Warren, B. E. and J. T. Burwell: The Structure of Rhombic Sulfur. J. Chem. Physics 3, 6 (1935).
Yakel, H. L., Jr. and E. W. Hughes: The Unit-cell Dimensions and Space Groups of Two Modifications of Crystalline Glycylglycylglycine. Acta Crystallogr. 5, 847 (1952).
The Structure of N,N’-Diglycyl-L-cystine Dihydrate. J. Amer. Chem. Soc. 74, 6302 (1952).
The Crystal Structure of N,N’-Diglycyl-L-cystine Dihydrate. Acta Crystallogr. 7, 291 (1954).
Zahn, H.: Über die Struktur des α-Keratins. Z. Naturforsch. 2 b, 104 (1947).
Zussman, J.: The Structure of Hydroxyproline. Acta Crystallogr. 4, 72 (1951).
Zussman, J.: The Structure of Hydroxyproline. Acta Crystallogr. 4, 493 (1951).
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Pauling, L., Corey, R.B. (1954). The Configuration of Polypeptide Chains in Proteins. In: Ƶechmeister, L. (eds) Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrés dans la Chimie des Substances Organiques Naturelles. Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products / Progrés dans la Chimie des Substances Organiques Naturelles, vol 11. Springer, Vienna. https://doi.org/10.1007/978-3-7091-8014-3_5
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