Crossref journal-article
Elsevier BV
Folding and Design (78)
Bibliography

Neira, J. L., & Rico, M. (1997). Folding studies on ribonuclease A, a model protein. Folding and Design, 2(1), R1–R11.

Authors 2
  1. José Luis Neira (first)
  2. Manuel Rico (additional)
References 70 Referenced 63
  1. 10.1016/0014-5793(93)81405-O / FEBS. Lett / Protein folding and stability: the pathway of folding of barnase by Fersht (1993)
  2. {'key': '10.1016/S1359-0278(97)00001-1_bib2', 'first-page': '81', 'article-title': 'Protein engineering in analysis of protein folding pathways and stability', 'volume': '202', 'author': 'Matouschek', 'year': '1991', 'journal-title': 'Methods Enzymol'} / Methods Enzymol / Protein engineering in analysis of protein folding pathways and stability by Matouschek (1991)
  3. 10.1016/S1359-0278(96)00003-X / Fold. & Des / On-pathway versus off-pathway folding intermediates by Baldwin (1996)
  4. 10.1146/annurev.bb.21.060192.001331 / Annu. Rev. Biophys. Biomol. Struct / Protein folding studied using hydrogen-exchange labelling and two-dimensional NMR by Englander (1992)
  5. 10.1016/0959-440X(93)90206-Z / Curr. Opin. Struct. Biol / Pulsed H/D exchange studies of folding intermediates by Baldwin (1993)
  6. 10.1016/S0959-440X(94)90067-1 / Curr. Opin. Struct. Biol / Protein engineering and the dissection of protein folding pathways by Serrano (1994)
  7. 10.1016/0959-440X(95)80012-P / Curr. Opin. Struct. Biol / Characterizing transition states in protein folding: an essential step in the puzzle by Fersht (1994)
  8. 10.1016/0968-0004(94)90171-6 / Trends Biol. Sci / Understanding protein folding – the lysozyme story so far by Dobson (1994)
  9. 10.1126/science.181.4096.223 / Science / Principles that govern the folding of protein chain (Nobel Lecture) by Anfinsen (1973)
  10. 10.1038/335694a0 / Nature / NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A by Udgaonkar (1988)
  11. 10.1073/pnas.87.21.8197 / Proc. Natl. Acad. Sci. USA / Early folding intermediate of ribonuclease A by Udgaonkar (1990)
  12. 10.1073/pnas.90.2.615 / Proc. Natl. Acad. Sci. USA / Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli by Laity (1993)
  13. 10.1021/bi00408a010 / Biochemistry / Structure of phosphate-free ribonuclease A refined at 1.26 Å by Wlodaver (1988)
  14. 10.1006/jmbi.1993.1075 / J. Mol. Biol / High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy by Santoro (1993)
  15. 10.1021/bi00046a016 / Biochemistry / Effects of naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A by Wang (1995)
  16. 10.1021/bi00462a019 / Biochemistry / pH dependence of the urea and guanidinium hydrochloride denaturation of ribonuclease A and ribonuclease T1 by Pace (1990)
  17. 10.1016/0959-440X(93)90203-W / Curr. Opin. Struct. Biol / Peptide conformation and protein folding by Dyson (1993)
  18. 10.1021/bi00779a019 / Biochemistry / Helix-coil transition of the isolated amino terminus of ribonuclease by Brown (1971)
  19. 10.1073/pnas.79.8.2470 / Proc. Natl. Acad. Sci. USA / A salt bridge stabilises the helix formed by isolated C-peptide of Rnase A by Bierzynski (1982)
  20. 10.1016/0014-5793(83)80779-0 / FEBS Lett / Low temperature 1H-NMR evidence of the folding of isolated ribonuclease S-peptide by Rico (1983)
  21. 10.1063/1.1730390 / J. Chem. Phys / Theory of the phase transition between helix and random-coils in polypeptide chains by Zimm (1959)
  22. 10.1063/1.1731802 / J. Chem. Phys / On the theory of helix-coil transition on polypeptides by Lifson (1961)
  23. 10.1021/ma00132a006 / Macromolecules / Helix-coil stability constants for the naturally occurring amino acids in water. 22. Histidine parameters from random poly(hydroxylbutyl)-glutamine-co-L-histidine by Sueki (1984)
  24. 10.1038/307329a0 / Nature / A helix stop signal in the isolated S-peptide of ribonuclease A by Kim (1984)
  25. 10.1016/0006-291X(84)90294-8 / Biochim. Biophys. Res. Commun / On the fundamental role of Glu2–…Arg10+ salt bridge in the folding of isolated ribonuclease A S-peptide by Rico (1984)
  26. 10.1016/0301-4622(90)88012-H / Biophys. Chem / The Glu2–… Arg10+ side-chain interaction in the C-peptide helix or ribonuclease A by Fairman (1990)
  27. 10.1002/bip.360250605 / Biopolymers / Thermodynamic parameters for the helix-coil thermal transition of ribonuclease A S-peptide and derivatives from 1H NMR data by Rico (1986)
  28. 10.1016/0022-2860(86)85128-6 / J. Mol. Struct / Quantum-chemical calculations of a proposed Phen-Hisn+4 stabilising interaction in peptide α-helices by Bermejo (1986)
  29. 10.1073/pnas.82.8.2349 / Proc. Natl. Acad. Sci. USA / Nature of the charged-group effect on the stability of the C-peptide helix by Shoemaker (1985)
  30. 10.1002/prot.340230203 / Proteins / Determination of the conformation of folding initiation sites in proteins by computer simulation by Avbelj (1995)
  31. 10.1016/0014-5793(87)80948-1 / FEBS Lett / 1H NMR and CD evidence of the folding of isolated ribonuclease 50–61 fragment by Jiménez (1987)
  32. 10.1111/j.1432-1033.1988.tb14171.x / Eur. J. Biochem / 1H-NMR assignment and folding of the isolated ribonuclease 21–42 fragment by Jiménez (1988)
  33. 10.1021/ma60064a038 / Macromolecules / A method for predicting nucleation sites for protein folding based on hydrophobic contacts by Matheson (1978)
  34. 10.1021/bi00245a004 / Biochemistry / Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: implications on a potential chain-folding initiation site by Beals (1991)
  35. {'key': '10.1016/S1359-0278(97)00001-1_bib35', 'first-page': '322', 'article-title': 'Solution structure of the isolated ribonuclease C-terminal 112–124 fragment', 'volume': '1038', 'author': 'Jiménez', 'year': '1990', 'journal-title': 'Biochem. Biophy. Acta'} / Biochem. Biophy. Acta / Solution structure of the isolated ribonuclease C-terminal 112–124 fragment by Jiménez (1990)
  36. 10.1021/bi00049a011 / Biochemistry / Analysis of the structure of ribonuclease A in native and partially denatured states by time-resolved non-radiative dynamic excitation energy transfer between site-specific extrinsic probes by Buckler (1995)
  37. 10.1021/ja00168a044 / J. Am. Chem. Soc / Local structure in ribonuclease A. Effect of amino acid substitutions on the preferential formation of the native disulfide loop in synthetic peptides corresponding to residues Cys 58–Cys 72 of bovine pancreatic ribonuclease A by Altmann (1990)
  38. 10.1021/ja00061a001 / J. Am. Chem. Soc / Energetic and structural basis for the preferential formation of the native disulfide loop involving Cys 65–Cys 72 in synthetic peptide fragments derived from the sequence of ribonuclease A by Talluri (1993)
  39. 10.1007/BF01024887 / J. Protein. Chem / Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser 50–Met 79 derived from bovine pancreatic ribonuclease A by Milburn (1988)
  40. 10.1021/bi00150a029 / Biochemistry / Denatured states of ribonuclease A have compact dimensions and residual secondary structure by Sosnick (1992)
  41. 10.1017/S0033583500005217 / Quart. Rev. Biophys / Hydrogen exchange and structural dynamics of proteins and nucleic acids by Englander (1984)
  42. {'issue': 'suppl 2', 'key': '10.1016/S1359-0278(97)00001-1_bib42', 'first-page': '237', 'article-title': 'Regeneration of bovine pancreatic ribonuclease A. Determination of two independent folding pathways', 'volume': '4', 'author': 'Rothwarf', 'year': '1995', 'journal-title': 'Protein Sci'} / Protein Sci / Regeneration of bovine pancreatic ribonuclease A. Determination of two independent folding pathways by Rothwarf (1995)
  43. 10.1016/S0021-9258(18)64177-8 / J. Biol. Chem / Studies of the reduction and reformation of protein disulfide bonds by Anfinsen (1961)
  44. 10.1016/S1359-0278(96)00053-3 / Fold. Des / Identification of disulfide bonds in the refolding of bovine pancreatic RNase A by Ruoppolo (1996)
  45. 10.1021/bi00061a027 / Biochemistry / Regeneration of bovine pancreatic ribonuclease A. I. Steady-state distribution by Rothwarf (1993)
  46. 10.1021/bi960090d / Biochemistry / Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A by Xu (1996)
  47. 10.1038/nsb0695-489 / Nat. Struct. Biol / Mechanism of reductive protein unfolding by Li (1995)
  48. 10.1021/bi00200a027 / Biochemistry / Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the unfolding and folding pathways by Talluri (1994)
  49. {'key': '10.1016/S1359-0278(97)00001-1_bib49', 'series-title': 'Mechanisms of Protein Folding', 'article-title': 'Early stages of protein folding', 'author': 'Roder', 'year': '1994'} / Mechanisms of Protein Folding / Early stages of protein folding by Roder (1994)
  50. 10.1016/0022-2836(79)90347-4 / J. Mol. Biol / The rate of inter conversion between the two unfolded forms of ribonuclease A does not depend on GdmCl concentration by Schmid (1979)
  51. 10.1021/bi00567a027 / Biochemistry / Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange by Kim (1980)
  52. 10.1021/bi00012a027 / Biochemistry / Nature of the early folding intermediate of ribonuclease A by Udgaonkar (1995)
  53. 10.1073/pnas.70.12.3347 / Proc. Natl. Acad. Sci. USA / Both the fast and slow refolding reactions of ribonuclease A yield native enzyme by Garel (1973)
  54. 10.1111/j.1432-1033.1981.tb06180.x / Eur. J. Biochem / A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A by Schmid (1981)
  55. {'key': '10.1016/S1359-0278(97)00001-1_bib55', 'series-title': 'Protein Folding', 'first-page': '197', 'article-title': 'Kinetics of unfolding and refolding of single-domain proteins', 'author': 'Schmid', 'year': '1989'} / Protein Folding / Kinetics of unfolding and refolding of single-domain proteins by Schmid (1989)
  56. 10.1073/pnas.92.7.2657 / Proc. Natl. Acad. Sci. USA / Kinetics and hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange by Kiefhaber (1995)
  57. 10.1016/S0065-3233(08)60129-1 / Adv. Protein Chem / Hydrogen-exchange in proteins by Hvidt (1966)
  58. 10.1038/375513a0 / Nature / Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A by Kiefhaber (1995)
  59. 10.1002/bip.360281003 / Biopolymers / Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition by Shakhnovich (1989)
  60. 10.1021/bi00693a026 / Biochemistry / Consideration of the possibility that the slow step in protein denaturation reactions is due to cis–trans isomerism of proline residues by Brandts (1975)
  61. 10.1002/pro.5560010710 / Protein Sci / Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding by mutation by Schultz (1992)
  62. 10.1021/bi00175a022 / Biochemistry / A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways by Houry (1994)
  63. 10.1021/bi960745a / Biochemistry / Nature of the unfolded state of ribonuclease A: effects of cis–trans X–Pro peptide bond isomerization by Houry (1996)
  64. 10.1021/bi952348q / Biochemistry / Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A by Dodge (1996)
  65. 10.1006/jmbi.1994.1446 / J. Mol. Biol / Generation of a non-prolyl cis peptide bond in ribonuclease T1 by Mayr (1994)
  66. 10.1038/nsb0695-495 / Nat. Struct. Biol / The nature of the initial step in the conformational folding of disulfide-intact ribonuclease by Houry (1995)
  67. 10.1021/bi960617m / Biochemistry / Circular dichroism evidence of the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A by Houry (1996)
  68. 10.1021/bi961085c / Biochemistry / Structure of the hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen–deuterium exchange by Houry (1996)
  69. 10.1021/bi961280r / Biochemistry / Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A by Sendak (1996)
  70. 10.1107/S0021889891004399 / J. Appl. Crystallogr / Molscript: a program to produce both detailed and schematic plots for protein structures by Kraulis (1991)
Dates
Type When
Created 20 years, 1 month ago (July 7, 2005, 11:24 a.m.)
Deposited 4 years, 1 month ago (July 13, 2021, 12:39 a.m.)
Indexed 1 month ago (July 30, 2025, 10:12 a.m.)
Issued 28 years, 7 months ago (Feb. 1, 1997)
Published 28 years, 7 months ago (Feb. 1, 1997)
Published Print 28 years, 7 months ago (Feb. 1, 1997)
Funders 0

None

@article{Neira_1997, title={Folding studies on ribonuclease A, a model protein}, volume={2}, ISSN={1359-0278}, url={http://dx.doi.org/10.1016/s1359-0278(97)00001-1}, DOI={10.1016/s1359-0278(97)00001-1}, number={1}, journal={Folding and Design}, publisher={Elsevier BV}, author={Neira, José Luis and Rico, Manuel}, year={1997}, month=feb, pages={R1–R11} }