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 Vega, M. C.
Right arrow Articles by Serrano, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vega, M. C.
Right arrow Articles by Serrano, L.
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 9, Issue 12 2322-2328, Copyright © 2000 by Cold Spring Harbor Laboratory Press

JOURNAL ARTICLE

Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot

MC Vega, JC Martinez and L Serrano
EMBL, Heidelberg, Germany.

Residue Asn47 at position L1 of a type II' beta-turn of the alpha-spectrin SH3 domain is located in a disallowed region of the Ramachandran plot (phi = 56 +/- 12, psi = -118 +/- 17). Therefore, it is expected that replacement of Asn47 by Gly should result in a considerable stabilization of the protein. Thermodynamic analysis of the N47G and N47A mutants shows that the change in free energy is small (approximately 0.7 kcal/mol; approximately 3 kJ/mol) and comparable to that found when mutating a Gly to Ala in a alpha-helix or beta-sheet. X-ray structural analysis of these mutants shows that the conformation of the beta-turn does not change upon mutation and, therefore, that there is no relaxation of the structure, nor is there any gain or loss of interactions that could explain the small energy change. Our results indicate that the energetic definition of II' region of the Ramachandran plot (phi = 60 +/- 30, psi = -115 +/- 15) should be revised for at least Ala and Asn in structure validation and protein design.
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
E. S. Cobos, A. M. Candel, and J. C. Martinez
An Error Analysis for Two-State Protein-Folding Kinetic Parameters and {varphi}-Values: Progress toward Precision by Exploring pH Dependencies on Leffler Plots
Biophys. J., June 1, 2008; 94(11): 4393 - 4404.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
L. Spagnolo, S. Ventura, and L. Serrano
Folding specificity induced by loop stiffness
Protein Sci., July 1, 2003; 12(7): 1473 - 1482.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. A. Grant, Z. Hu, and X. L. Xu
Amino Acid Residue Mutations Uncouple Cooperative Effects in Escherichia coliD-3-Phosphoglycerate Dehydrogenase
J. Biol. Chem., May 18, 2001; 276(21): 17844 - 17850.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.