| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophys J, December 2002, p. 2981-2986, Vol. 83, No. 6
Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104, USA
The discrepancy of the pH dependence of the unfolding
free energy for staphylococcal nuclease from what is expected from an idealized model for the unfolded state is accounted for by the recently
developed Gaussian-chain model. Residual electrostatic effects in the
unfolded state are attributed to nonspecific interactions dominated by
charges close along the sequence. The dominance of nonspecific local
interactions appears to be supported by some experimental evidence.
Biophys J, December 2002, p. 2981-2986, Vol. 83, No. 6
© 2002 by the Biophysical Society 0006-3495/02/12/2981/06 $2.00
This article has been cited by other articles:
![]() |
N. C. Fitzkee and B. Garcia-Moreno E Electrostatic effects in unfolded staphylococcal nuclease Protein Sci., February 1, 2008; 17(2): 216 - 227. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Lindman, S. Linse, F. A. A. Mulder, and I. Andre pKa Values for Side-Chain Carboxyl Groups of a PGB1 Variant Explain Salt and pH-Dependent Stability Biophys. J., January 1, 2007; 92(1): 257 - 266. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Tollinger, K. A. Crowhurst, L. E. Kay, and J. D. Forman-Kay Site-specific contributions to the pH dependence of protein stability PNAS, April 15, 2003; 100(8): 4545 - 4550. [Abstract] [Full Text] [PDF] |
||||
![]() |
H.-X. Zhou and F. Dong Electrostatic Contributions to the Stability of a Thermophilic Cold Shock Protein Biophys. J., April 1, 2003; 84(4): 2216 - 2222. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |