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 PETRESCU, A. J.
Right arrow Articles by SMITH, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by PETRESCU, A. J.
Right arrow Articles by SMITH, J. 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 6 1396-1403, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Excluded volume in the configurational distribution of a strongly-denatured protein

A. J. PETRESCU, V. RECEVEUR, P. CALMETTES, D. DURAND and J. C. SMITH
Institute of Biochemistry, 77700 Bucharest 17, Romania Laboratoire Leon Brillouin, CEA-Saclay, 91191 Gif sur Yvette, France

The configurational distribution of phosphoglycerate kinase (PGK) strongly-denatured in 4M guanidine hydrochloride solution is investigated using small-angle neutron scattering (SANS) and Monte Carlo computer simulation. It is shown that the experimental scattering profile can be represented by a random flexible chain of spheres of excess scattering density with excluded volume interactions, the best agreement being achieved when partial sphere intersection is allowed. The radius of gyration of the chain increases by a factor of 4 on denaturation, whereas the average length of segments ~5 residues long increases by only ~10%, consistent with a picture in which the large expansion on denaturation originates primarily from increased long-range flexibility of the polypeptide chain. The results provide a description of the chain statistics from which the construction of starting points for simulation studies of folding of the protein can be envisaged.
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
J. E. Kohn, I. S. Millett, J. Jacob, B. Zagrovic, T. M. Dillon, N. Cingel, R. S. Dothager, S. Seifert, P. Thiyagarajan, T. R. Sosnick, et al.
Random-coil behavior and the dimensions of chemically unfolded proteins
PNAS, August 24, 2004; 101(34): 12491 - 12496.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
T. Huynh, J. C. Smith, and A. Sanson
Protein Unfolding Transitions in an Intrinsically Unstable Annexin Domain: Molecular Dynamics Simulation and Comparison with Nuclear Magnetic Resonance Data
Biophys. J., August 1, 2002; 83(2): 681 - 698.
[Abstract] [Full Text] [PDF]


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