Protein Science Sheba protein
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
Right arrow Citation Map
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 GUPTA, P.
Right arrow Articles by VOEGLER, A. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by GUPTA, P.
Right arrow Articles by VOEGLER, A. C.
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 7, Issue 12 2642-2652, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Effect of denaturant and protein concentrations upon protein refolding and aggregation: A simple lattice model

P. GUPTA, C. K. HALL and A. C. VOEGLER
Department of Chemical Engineering, Box 7905, North Carolina State University, Raleigh, North Carolina 27695

We present a study of the competition between protein refolding and aggregation for simple lattice model proteins. The effect of solvent conditions (i.e., the denaturant concentration and the protein concentration) on the folding and aggregation behavior of a system of simple, two-dimensional lattice protein molecules has been investigated via dynamic Monte Carlo simulations. The population profiles and aggregation propensities of the nine most populated intermediate configurations exhibit a complex dependence on the solution conditions that can be understood by considering the competition between intra- and interchain interactions. Some of these configurations are not even seen in isolated chain simulations; they are observed to be highly aggregation prone and are stabilized primarily by the aggregation reaction in multiple-chain systems. Aggregation arises from the association of partially folded intermediates rather than from the association of denatured random-coil states. The aggregation reaction dominates over the folding reaction at high protein concentration and low denaturant concentration, resulting in low refolding yields at those conditions. However, optimum folding conditions exist at which the refolding yield is a maximum, in agreement with some experimental observations.
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
 Proc. Natl. Acad. Sci. USAHome page
B. W. Zhang, D. Jasnow, and D. M. Zuckerman
Efficient and verified simulation of a path ensemble for conformational change in a united-residue model of calmodulin
PNAS, November 13, 2007; 104(46): 18043 - 18048.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
R. Schwartz and J. King
Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure
Protein Sci., January 1, 2006; 15(1): 102 - 112.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Cellmer, D. Bratko, J. M. Prausnitz, and H. Blanch
Protein-folding landscapes in multichain systems
PNAS, August 16, 2005; 102(33): 11692 - 11697.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
J. M. Finke, M. S. Cheung, and J. N. Onuchic
A Structural Model of Polyglutamine Determined from a Host-Guest Method Combining Experiments and Landscape Theory
Biophys. J., September 1, 2004; 87(3): 1900 - 1918.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
K. Leonhard, J. M. Prausnitz, and C. J. Radke
Solvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kinetics
Protein Sci., February 1, 2004; 13(2): 358 - 369.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
H. Jang, C. K. Hall, and Y. Zhou
Thermodynamics and stability of a {beta}-sheet complex: Molecular dynamics simulations on simplified off-lattice protein models
Protein Sci., January 1, 2004; 13(1): 40 - 53.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
H. Jang, C. K. Hall, and Y. Zhou
Assembly and Kinetic Folding Pathways of a Tetrameric {beta}-Sheet Complex: Molecular Dynamics Simulations on Simplified Off-Lattice Protein Models
Biophys. J., January 1, 2004; 86(1): 31 - 49.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
H. Jang, C. K. Hall, and Y. Zhou
Protein Folding Pathways and Kinetics: Molecular Dynamics Simulations of beta -Strand Motifs
Biophys. J., August 1, 2002; 83(2): 819 - 835.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
R.I. Dima and D. Thirumalai
Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
Protein Sci., May 1, 2002; 11(5): 1036 - 1049.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
R. Schwartz, S. Istrail, and J. King
Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues
Protein Sci., May 1, 2001; 10(5): 1023 - 1031.
[Abstract] [Full Text]

Home page
 Protein Sci.Home page
P. M. Harrison, H. S. Chan, S. B. Prusiner, and F. E. Cohen
Conformational propagation with prion-like characteristics in a simple model of protein folding
Protein Sci., April 1, 2001; 10(4): 819 - 835.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by The Protein Society.