Understanding conserved amino acids in proteins

Physica A: Statistical Mechanics and its Applications

Volumn 314, Issue 1-4, 2002, Pages 600-606

  Dokholyan, Nikolay V ^a   Mirny, Leonid A ^a,b   Shakhnovich, Eugene I ^a  

^a HARVARD UNIVERSITY   (United States)

^b HARVARD MIT DIVISION OF HEALTH SCIENCES AND TECHNOLOGY   (United States)

Author keywords

Conserved amino acids; Model; Protein evolution

Indexed keywords

PRESSURE EFFECTS; PROTEINS; REACTION KINETICS; THERMODYNAMICS;

CONSERVATISM PATTERNS;

AMINO ACIDS;

EID: 0036950560     PISSN: 03784371     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4371(02)01079-8     Document Type: Conference Paper

References (26)

1. Branden C., Tooze J. Introduction to Protein Structure. 1998;Garland Publishing Inc. New York.
2. Mirny L.A., Shakhnovich E.I. J. Mol. Biol. 291:1999;177.
3. Dokholyan N.V., Shakhnovich E.I. J. Mol. Biol. 312:2001;289.
4. Ptitsyn O.B. J. Mol. Biol. 278:1998;655.
5. Mirny L.A., Abkevich V.I., Shakhnovich E.I. Proc. Natl. Acad. Sci. USA. 95:1998;4976.
6. van Nuland N.A.J., Chiti H., Taddei N., Raugei G., Ramponi G., Dobson C. J. Mol. Biol. 283:1998;883.
7. van Nuland N.A.J., Meijberg W., Warner J., Forge V., Scheek R., Robbilard G., Dobson C. Biochemistry. 37:1998;622.
8. Dokholyan N.V., Buldyrev S.V., Stanley H.E., Shakhnovich E.I. J. Mol. Biol. 296:2000;1183.
9. Sali A., Shakhnovich E.I., Karplus M. J. Mol. Biol. 235:1994;1614.
10. Shakhnovich E.I., Gutin A.M. Proc. Natl. Acad. Sci. USA. 90:1993;7195.
11. Ramanathan S., Shakhnovich E.I. Phys. Rev. E. 50:1994;1303.
12. Finkelstein A.V., Gutin A., Badretdinov A. Proteins. 23:1995;142.
13. Pande V.S., Grosberg A.Y., Tanaka T. Phys. Rev. E. 51:1995;3381.
14. Bowie J.U., Luthy R., Eisenberg D. Science. 253:1991;164.
15. Holm L., Sander C. J. Mol. Biol. 233:1993;123.
16. Rost B. Folding Des. 2:1997;S19.
17. Tiana G., Broglia R., Shakhnovich E.I. Proteins: Struct. Funct. Genet. 39:2000;244.
18. Dodge C., Schneider R., Sander C. Nucl. Acid Res. 26:1998;313.
19. Press W.H., Flannery B.P., Teukolsky S.A., Vetterling W.T. Numerical Recipes. 1989;Cambridge University Press, Cambridge.
20. Itzhaki L.S., Otzen D.E., Fersht A.R. J. Mol. Biol. 254:1995;260.
21. Hamill S.J., Steward A., Clarke J. J. Mol. Biol. 297:2000;165.
22. López-Hernández E., Serrano L. Folding Des. 1:1996;43.
23. Jernigan R.L., Bahar I. Curr. Opinion Struct. Biol. 6:1996;195.
24. Miyazawa S., Jernigan R.L. Proteins. 34:1999;49. (Table V.).
25. F.C. Bernstein, T.F. Koetzle, G.J.B. Williams, E.F.M. Jr., M.D. Brice, J.R. Rodgers, O. Kennard, T. Shimanouchi, M. Tasumi, J. Mol. Biol. 112 (1977) 535.
26. E.E. Abola, F.C. Bernstein, S.H. Bryant, T.F. Koetzle, J. Weng, in: F.H. Allen, G. Bergerhoff, R. Sievers (Eds.), Crystallographic Databases-Information Content, Software Systems, Scientific Applications, Data Commission of the International Union of Crystallography, Cambridge, 1987, pp. 107-132.