Are buried salt bridges important for protein stability and conformational specificity?

Nature Structural Biology

Volumn 2, Issue 2, 1995, Pages 122-128

  Waldburger, Carey D ^a   Schildbach, Joel F ^a   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REPRESSOR PROTEIN;

ARTICLE; DNA BINDING; HYDROPHOBICITY; MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACIDS; BACTERIOPHAGE P22; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DNA, VIRAL; HYDROGEN BONDING; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OPERATOR REGIONS (GENETICS); PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; VIRAL PROTEINS;

EID: 0029564595     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0295-122     Document Type: Article

References (28)

1. Barlow, DJ. &Thornton, J.M. Ion-pairs in proteins./molec. Biol. 168, 867-885 (1983).
2. Perutz, M. &Raidt, H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 255, 256-259 (1975).
3. Perutz, M. Electrostatic effects in proteins. Science 201, 11871 191 (1978).
4. Ruegg, C., Ammer, D. &Lerch, K. Comparison of amino acid sequence and thermostability of tyrosinase from three wild type strains of Neurospora crassa. J. biol. Chem. 257, 6420-6426 (1982).
5. Fersht, A.R. Conformational equilibria in a- and 8- chymotrypsin. The energetics and importance of the salt bridge. J. molec. Biol. 64, 497-509 (1972).
6. Anderson, D.E., Becktel, W.J. &Dahlquist, F.W. pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29, 2403-2408 (1990).
7. Horovitz, A., Serrano, L, Avron, B., Bycroft, M. &Fersht, A.R. Strength and co-operativity of contributions of surface salt bridges to protein stability. J. molec. Biol. 216, 1031-1044 (1990).
8. Erwin, C.R., Barnett, B.L., Oliver, J.D. &Sullivan, J.F. Effects of engineered salt bridges on the stability of subtilisin BPN'. Prof. Engng. 4,87-97 (1990).
9. Sali, D., Bycroft, M. &Fersht, A.R. Surface electrostatic interactions contribute little to stability of barnase. J. molec. Biol. 220, 779-778 (1991).
10. Dao-Pin, S., Sauer, U., Nicholson, H. &Matthews, B.W. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30, 7142-7153 (1991).
11. Hendsch, Z.S. &Tidor, B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Prof Sci. 3, 21 1-226 (1994).
12. Raumann, B.E., Rould, M.A., Pabo, C.O. &Sauer, R.T. DNA recognition by p-sheets in the Arc repressor-operator crystal structure. Nature 367, 754-757 (1994).
13. Vershon, A.K., Bowie, J.U., Karplus, T.M. &Sauer, R.T. Isolation and analysis of Arc repressor mutants: Evidence for an unusual mechanism of DNA binding. Proteins 1, 302-31 1 (1986).
14. Bowie, J.U. &Sauer, R.T. Identifying determinants of folding and activity for a protein of unknown structure. Proc. natn. Acad. Sci. U.S.A. 86, 2152-2156 (1989).
15. Milla, M.E., Brown, B.M. &Sauer, R.T. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature struct Biol. 1, 518-523 (1994).
16. Brown, B.M., Milia, M.E., Smith, T.L. &Sauer, R.T. Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition. Nature struct. Biol. 1, 164-168 (1994).
17. Horovitz, A. &Fersht, A.R. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. molec. Biol. 214,613-617(1990).
18. Bowie, J.U. &Sauer, R.T. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28, 7139-7143 (1989).
19. Chothia, C. The nature of the accessible and buried surfaces in proteins. 7. molec. Biol. 105, 1-14(1976).
20. O'Shea, E.K., Klemm, J.D., Kim, P.S. &Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539-544(1991).
21. Harbury, P. B., Zhang, T, Kim, P. S. &Alber, T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407 (1993).
22. Milla, M.E., Brown, B.M. &Sauer, R.T. P22 Arc repressor: Enhanced expression of unstable mutants by addition of polar C-terminal sequences. Prof Sci. 2, 2198-2205 (1993).
23. Bowie, J.U. &Sauer, R.T. Identification of C-terminal extensions that protect proteins from intracellular proteolysis. J. biol. Chem. 264, 7596-7602 (1989).
24. Brown, B.M. &Sauer, R.T. Assembly of the Arc repressor-operator complex: Cooperative interactions between DNA-bound dimers. Biochemistry 32, 1354-1363 (1993).
25. Milla, M.E. &Sauer, R.T. P22 Arc repressor: Folding kinetics of a single-domain, dimeric protein. Biochemistry 33, 1125-1 133 (1994).
26. Breg, J.N., van Opheusden, J.H.J., Burgering, M.J., Boelens, R. &Kaptein, R. Structure of Arc repressor in solution: Evidence for a family of β-sheet DNA-binding proteins. Nature 346, 586-589 (1990).
27. Bonvin, A.M.J.J., Vis, H., Breg, J.N., Burgering, M.J.M., Boelens, R. &Kaptein, R. Nuclear magnetic resonance solution structure of the Arc repressor using relaxation matrix calculations. J. molec. Biol. 236, 328-341 (1994).
28. Chakrabartty, A., Kortemme, T, Padmanabhan, S. &Baldwin, R.L. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32, 5560-5565 (1993).