Protein stability: Still an unsolved problem

Cellular and Molecular Life Sciences

Volumn 53, Issue 10, 1997, Pages 790-802

  Richards, F M ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

Cavities and stability; Packing; Protein structure

Indexed keywords

AMINO ACID;

GENE MUTATION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; THERMOSTABILITY;

AMINO ACIDS; DISULFIDES; DRUG STABILITY; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEINS; THERMODYNAMICS;

EID: 0030690394     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050100     Document Type: Review

References (25)

1. Fruton .J. S. (1972) Molecules and life, Wiley-Interscience. New York
2. Bullough P. A., Hughson F. M., Skehel .J. J. and Wiley D. C. (1994) Structure of influenza hemaggfutinin at the pH of membrane fusion. Nature 371: 37-43
3. Matthew J. B. and Richards F. M. (1982) Anion binding and pH dependent electrostatic effects in ribonuclease. Biochemistry 21: 4989-4999
4. Hermans J. and Scheraga H. A. (1961) Structural studies of ribonuclease, V. Reversible change of configuration. J. Am. Chem. Soc. 83: 3283-3292
5. Kitaigordosky A. I. (1961) Organic Chemical Crystallography. Consultants Bureau. New York (authorized English translation 1961. original Russian text published 1955)
6. Kitaigordosky A. I. (1473) Molecular crystals and molecules. Academic Press. New York
7. Richards F. M. and Lim W. A. (1994) An analysis of packing in the protein folding problem. Quart. Rev. Biophys, 26: 423-498
8. Ponder J. W. and Richards F. M. (1987) Tertiary template for proteins use of packing criteria in the enumeration of allowed sequences for different structural classes J. Molec. Biol. 193: 775-791
9. Terwilliger T. C. (1995) Engineering the stability and function of gene V protein. Adv. Protein Chem. 46: 177-216
10. Sandberg N. S. and Terwilliger T. C. (1991) Energetics of repacking a protein. Proc. Natl Acad. Sci. USA 88: 1706-1710
11. Eriksson A. F., Baase W. A., Zhang X.-J., Heinz D. W., Blaber M., Baldwin E. P. et al. (1942) Response of a protein structure to easily-creating mutations and its relationship to the hydrophobic effect, Science 255: 178-183
12. Eriksson A. E., Baase W. A. and Matthews B. W. (1993) Similar hydrophobie replacements of Leu 99 and Phe 153 within the core of T. lysozyme have different structural and thermodynamic consequences. J. Molec. Biol. 229: 747-769
13. Hellinga H. W., Wynn R. and Richards F. M. (1992) The hydrophobie core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions. Biochemistry 31: 11203-11209
14. DeLorimier R., Hellinga H. W. and Spicer L. D. (1996) NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin. Protein Sci. 5: 2552-2565
15. Varadarajan R. and Richards F. M. (1992) Crystallographic structures of ribonuclease-S variants with non polar substitution of position 13: packing and cavities. Biochemistry 31: 12315-12327
16. Thomson J., Ratnaparkhi G. S., Varadarajan R., Sturtevanl J. M. and Richards F. M. (1994) Thermodynamic, and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S. Biochemistry 33: 8587-8593
17. Connelly P. R., Varadarajan R., Sturtevant J. M. and Richards F. M. (1990) Thermodynamics of protein-peptide interactions in their ribonuclease-S system studies by titration calorimetry. Biochemistry 29: 6108-6114
18. DiCera E. (1997) Site-specific linkage thermodynamics. Adv. Protein Chem. (in press)
19. Shortle D., Wang Y., Gillespie J. R. and Wrabl J. O. (1996) Protein folding for realists: a timeless phenomenon. Protein Sci. 5: 991-1000
20. Wynn R., Harkins P. C., Richards F. M. and Fox R. O. (1996) Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Protein Sci. 5: 1026-1031
21. Wynn R., Harkins P. C., Richards F. M. and Fox R. O. (1997) Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease. Protein Sci. 6: 1621-1626
22. Wynn R. and Richards F. M. (1993) Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in E. coli thioredoxin does not affect the unfolded state. Biochemistry 32: 12922-12927
23. Wynn R., Anderson C. L., Richards F. M. and Fox R. O. (1995) Interactions in nonnative and truncated forms of staphylococcal nuclease as indicated by mutational free energy changes. Protein Sci. 4: 1815-1823
24. DeDecker B. S., O'Brien R., Fleming P. J., Geiger J. H., Jackson S. P. and Sigler P. B. (1996) The crystal structure of a hyperthermophilic archeal TATA-box binding protein. J. Molec. Biol. 264: 1072-1084
25. St. Clair N. L. and Navia M. A. (1992) Cross-linked enzyme crystals as robust catalysts. J. Am. Chem. Soc. 114: 7314-7316