Salt bridges and conformational flexibility: Effect on protein stability

Biotechnology and Biotechnological Equipment

Volumn 22, Issue 1, 2008, Pages 606-611

  Karshikoff, A ^a   Jelesarov, I ^b  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Electrostatic interactions; Modelling; Proteins; Salt bridges; Stability

Indexed keywords

EID: 41049084982     PISSN: 13102818     EISSN: None     Source Type: Journal    
DOI: 10.1080/13102818.2008.10817520     Document Type: Article

References (28)

1. Anderson, D.E., Becktel, W.J., Dahlquist, F.W., (1990) Biochemistry 29 2403–22408.
2. Antosiewicz, J., McCammon, J.A., Gilson, M.K., (1996) Biochemistry 35 7819–7833.
3. Baptista, A.M., Teixeira, V.H., Soares, C.M., (2002) J. Chem. Phys. 117 4184–4200.
4. Barlow, D.J., Thornton, J.M., (1983) J. Mol. Biol. 168 867–885.
5. Bashford, D., Gerwert, K., (1992) J. Mol. Biol. 224 473–486.
6. Bjelic, S., Karshikoff, A., Jelesarov, I., (2006) Biochemistry 45 8931–8939.
7. Bjelic, S., Wieninger, S., Jelesarov, I., Karshikoff, A., (2007) Proteins in press
8. Dragan, A.I., Potekhin, S.A., Sivolob, A., Lu, M., Privalov, P.L., (2004) Biochemistry 43 14891–14900.
9. Gorfe, A.A., Ferrara, P., Caflisch, A., Marti, D.N., Bosshard, H.R., Jelesarov, I., (2002) Proteins 46 41–60.
10. Hwang, J.-K., Warshel, A., (1988) Nature 334 270–272.
11. Jeffrey G.A., (1977) An introduction to hydrogen bonding, Oxford University Press, New York
12. Karshikoff, A., (1995) Protein Eng. 8 243–248.
13. Karshikoff A., (2006) Non-covalent interactions in proteins, Imperial College Press, London
14. Koumanov, A., Karshikoff, A., Friis, E.P., Borchert, T.V., (2001) J. Phys. Chem. B 105 9339–9344.
15. Kundrotas P., Karshikoff A., (2004) Electrostatic interactions in unfolded proteins. Implication for protein stability. in:Current Topics in Peptide & Protein Research (Richard R., Ed.) Research Trends, Poojapura, 6 21–35.
16. Langella, E., Improta, R., Crescenzi, O., Barone, V., (2006) Proteins 64 167–177.
17. Lyu, P.C.C., Gans, P.J., Kallenbach, N.R., (1992) J. Mol. Biol. 223 343–350.
18. Phelan, P., Gorfe, A.A., Jelesarov, I., Marti, D.N., Warwicker, J., Bosshard, H.R., (2002) Biochemistry 41 2998–3008.
19. Ren, B., Tibbelin, G., Pascale, D., Rossi, M., Bartolucci, S., Ladenstein, R., (1998) Nat. Struct. Biol. 5 602–611.
20. Tanford, C., Kirkwood, J.G., (1957) JACS 79 5333–5339.
21. Teixeira, V.H., Cunha, C.A., Machuqueiro, M., Oliveira, A.S.F., Victor, B.L., Soares, C.M., Baptista, A.A., (2005) J. Phys. Chem. 109 14691–14706.
22. van Vlijmen, H.W.T., Schaefer, M., Karplus, M., (1998) Proteins 33 145–158.
23. Vanvlijmen, H.W.T., Curry, S., Schaefer, M., Karplus, M., (1999) J. Mol. Biol. 275 295–308.
24. Warshel, A., Russell, S.T., Churg, A.K., (1984) Proceedings of the National Academy of Sciences of the United States of America 81 4785–4789.
25. Xue, W.F., Szczepankiewicz, O., Bajer, M.C., Thulin, E., Linse, S., (2006) J. Mol. Biol. 358 1244–1255.
26. Yang, A.-S., Honig, B., (1993) J. Mol. Biol. 231 459–474.
27. Yang, A.-S., Honig, B., (1994) J. Mol. Biol. 237 602–614.
28. Zhou, H.-X., Vijayakumar, M., (1997) J. Mol. Biol. 267 1002–1011.