Principles that govern the folding of protein chains.

Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for "their contribution to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule." In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the "Thermodynamic Hypothesis," and outlined potential avenues of current and future scientific exploration.

[1]  M. L. Anson.  Protein Denaturation and the Properties of Protein Groups , 1945 .

[2]  Henry Eyring,et al.  Conformation Changes of Proteins , 1954 .

[3]  C. Anfinsen,et al.  Reductive cleavage of disulfide bridges in ribonuclease. , 1957, Science.

[4]  F. Richards.  ON THE ENZYMIC ACTIVITY OF SUBTILISIN-MODIFIED RIBONUCLEASE. , 1958, Proceedings of the National Academy of Sciences of the United States of America.

[5]  C. Anfinsen,et al.  SOME RELATIONSHIPS OF STRUCTURE TO FUNCTION IN RIBONUCLEASE , 1959, Annals of the New York Academy of Sciences.

[6]  S. Moore,et al.  The sequence of the amino acid residues in performic acid-oxidized ribonuclease. , 1960, The Journal of biological chemistry.

[7]  White Fh,et al.  Regeneration of native secondary and tertiary structures by air oxidation of reduced ribonuclease. , 1961 .

[8]  H. Dintzis.  Assembly of the peptide chains of hemoglobin. , 1961, Proceedings of the National Academy of Sciences of the United States of America.

[9]  C. Anfinsen,et al.  The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. , 1961, Proceedings of the National Academy of Sciences of the United States of America.

[10]  C. Anfinsen,et al.  Side-chain interactions governing the pairing of half-cystine residues in ribonuclease. , 1962, The Journal of biological chemistry.

[11]  C. Anfinsen,et al.  A reinvestigation of the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. , 1962, The Journal of biological chemistry.

[12]  C. Epstein,et al.  The Genetic Control of Tertiary Protein Structure: Studies With Model Systems , 1963 .

[13]  C. Anfinsen,et al.  NONUNIFORM LABELING OF EGG WHITE LYSOZYME. , 1963, Biochemistry.

[14]  C. Anfinsen,et al.  The identification of ureactive amino groups in ribonuclease and their significance to enzymatic activity. , 1963, The Journal of biological chemistry.

[15]  C. Epstein,et al.  Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. , 1963, The Journal of biological chemistry.

[16]  F. B. Straub,et al.  The enzymic reactivation of reduced ribonuclease. , 1963, Biochimica et biophysica acta.

[17]  S. Moore,et al.  The sequence of amino acid residues in bovine pancreatic ribonuclease: revisions and confirmations. , 1963, The Journal of biological chemistry.

[18]  R. B. Merrifield.  Automated synthesis of peptides. , 1965, Science.

[19]  J. C. Kendrew,et al.  Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence , 1965 .

[20]  G. Zanetti,et al.  Studies on polypeptides. XXXIV. Enzymic properties of partially synthetic De(16-20)- and De(15-20)-ribonucleases S'1-3. , 1966, Journal of the American Chemical Society.

[21]  R. Goldberger,et al.  Purification and properties of an enzyme from beef liver which catalyzes sulfhydryl-disulfide interchange in proteins. , 1966, The Journal of biological chemistry.

[22]  C. Epstein,et al.  Role of the Amino-Acid ‘Code’ and of Selection for Conformation in the Evolution of Proteins , 1966, Nature.

[23]  C. Anfinsen,et al.  Studies on the mechanism of the enzymic catalysis of disulfide interchange in proteins. , 1967, The Journal of biological chemistry.

[24]  D. Steiner.  Evidence for a precursor in the biosynthesis of insulin. , 1967, Transactions of the New York Academy of Sciences.

[25]  L. Moroder,et al.  Synthesis of peptide analogs of the N-terminal eicosapeptide sequence of ribonuclease A. VII. Synthesis of Ile8, Orn10- and Ala8, Orn10-eicosapeptides , 1967 .

[26]  C. Anfinsen,et al.  Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments. , 1967, Proceedings of the National Academy of Sciences of the United States of America.

[27]  R. Chance,et al.  Porcine Proinsulin: Characterization and Amino Acid Sequence , 1968, Science.

[28]  Ligand-induced resistance of staphylococcal nuclease and nuclease-T to proteolysis by subtilisin, alpha-chymotrypsin, and thermolysin. , 1969, The Journal of biological chemistry.

[29]  D. Veber,et al.  Studies on the total synthesis of an enzyme. V. The preparation of enzymatically active material. , 1969, Journal of the American Chemical Society.

[30]  C. Anfinsen,et al.  Purification of synthetic ribonuclease S-peptide derivatives by specific complex formation on columns of ribonuclease S-protein bound to agarose. , 1969, The Journal of biological chemistry.

[31]  A. Schechter,et al.  Hydrogen exchange in proteins as a measure of solvent exclusion due to ligands. Nuclease and myoglobin. , 1969, The Journal of biological chemistry.

[32]  C B Anfinsen,et al.  An experimental approach to the study of the folding of staphylococcal nuclease. , 1969, The Journal of biological chemistry.

[33]  I. Kato,et al.  Soybean trypsin inhibitor‐C: An active derivative of soybean trypsin inhibitor composed of two noncovalently bonded peptide fragments , 1970, FEBS letters.

[34]  A. W. Hanson,et al.  The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A. , 1970, The Journal of biological chemistry.

[35]  C. Anfinsen,et al.  Semisynthetic analogues of an enzymically active complex formed between two overlapping fragments of staphylococcal nuclease. , 1971, The Journal of biological chemistry.

[36]  R. B. Merrifield,et al.  The synthesis of ribonuclease A. , 1971, The Journal of biological chemistry.

[37]  C. Anfinsen,et al.  Solic phase synthetic study of the active site region of staphylococcal nuclease-T'. , 1971, The Journal of biological chemistry.

[38]  A. Schechter,et al.  Folding of staphylococcal nuclease: magnetic resonance and fluorescence studies of individual residues. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[39]  Staphylococcal nuclease (Foggi strain). II. The amino acid sequence. , 1971, The Journal of biological chemistry.

[40]  J. Richardson,et al.  A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing. , 1971, The Journal of biological chemistry.

[41]  A. Schechter,et al.  Folding of staphylococcal nuclease: kinetic studies of two processes in acid renaturation. , 1971, Journal of molecular biology.

[42]  C. Anfinsen,et al.  Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nuclease. , 1971, The Journal of biological chemistry.

[43]  I. Chaiken,et al.  Purification and properties of semisynthetic staphylococcal nuclease-T'. , 1971, The Journal of biological chemistry.

[44]  H. Scheraga.  Theoretical and experimental studies of conformations of polypeptides. , 1971, Chemical reviews.

[45]  A. Schechter,et al.  Inactivation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic determinant. , 1972, Biochemistry.

[46]  C B Anfinsen,et al.  An immunologic approach to the conformational equilibria of polypeptides. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[47]  A. Schechter,et al.  Antibodies to a distinct antigenic determinant of staphylococcal nuclease. , 1972, Journal of immunology.

[48]  The examination of the presence of amide groups in glutamic acid and aspartic acid residues of staphylococcal nuclease (Foggi strain). , 1972, The Journal of biological chemistry.

[49]  A comparison of the x-ray diffraction patterns of crystals of reconstituted nuclease-T and of native staphylococcal nuclease. , 1972, The Journal of biological chemistry.