Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by CAMACHO, C. J.
Right arrow Articles by THIRUMALAI, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by CAMACHO, C. J.
Right arrow Articles by THIRUMALAI, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 5, Issue 9 1826-1832, Copyright © 1996 by Cold Spring Harbor Laboratory Press

ARTICLE

Denaturants can accelerate folding rates in a class of globular proteins

C. J. CAMACHO and D. THIRUMALAI
Facultad de Fisica, Pontifica Universidad Catolica de Chile, Casilla 306, Santiago 22 Chile

We present a lattice Monte Carlo study to examine the effect of denaturants on the folding rates of simplified models of proteins. The two-dimensional model is made from a three-letter code mimicking the presence of hydrophobic, hydrophilic, and cysteine residues. We show that the rate of folding is maximum when the effective hydrophobic interaction {epsilon}(H) is approximately equal to the free energy gain {epsilon}(S) upon forming disulfide bonds. In the range 1 <= {epsilon}(H)/{epsilon}(S) <= 3, multiple paths that connect several intermediates to the native state lead to fast folding. It is shown that at a fixed temperature and {epsilon}(S) the folding rate increases as {epsilon}(H) decreases. An approximate model is used to show that {epsilon}(H) should decrease as a function of the concentration of denaturants such as urea or guanidine hydrochloride. Our simulation results, in conjunction with this model, are used to show that increasing the concentration of denaturants can lead to an increase in folding rates. This occurs because denaturants can destabilize the intermediates without significantly altering the energy of the native conformation. Our findings are compared with experiments on the effects of denaturants on the refolding of bovine pancreatic trypsin inhibitor and ribonuclease T1. We also argue that the phenomenon of denaturant-enhanced folding of proteins should be general.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
B. Patel and J. M. Finke
Folding and Unfolding of {gamma}TIM Monomers and Dimers
Biophys. J., October 1, 2007; 93(7): 2457 - 2471.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
J. M. Finke and J. N. Onuchic
Equilibrium and Kinetic Folding Pathways of a TIM Barrel with a Funneled Energy Landscape
Biophys. J., July 1, 2005; 89(1): 488 - 505.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. E. Otzen and M. Oliveberg
Salt-induced detour through compact regions of the protein folding landscape
PNAS, October 12, 1999; 96(21): 11746 - 11751.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Pan, D. Thirumalai, and S. A. Woodson
Magnesium-dependent folding of self-splicing RNA: Exploring the link between cooperativity, thermodynamics, and kinetics
PNAS, May 25, 1999; 96(11): 6149 - 6154.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by The Protein Society.