FASEB J.
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 Sauer, R. T.
Right arrow Articles by Schildbach, J. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sauer, R. T.
Right arrow Articles by Schildbach, J. F.

The FASEB Journal, Vol 10, 42-48, Copyright © 1996 by The Federation of American Societies for Experimental Biology

REVIEWS

Sequence determinants of folding and stability for the P22 Arc repressor dimer

RT Sauer, ME Milla, CD Waldburger, BM Brown and JF Schildbach
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

The Arc repressor is a small, homodimeric protein. Studies of mutant proteins show that the side chains that form the hydrophobic core are the most important determinants of structure. A variety of hydrogen bonds and salt bridges also contribute to stabilization of the native structure, but these can often be replaced by hydrophobic interactions. The transition state for folding/unfolding is dimeric and contains a large amount of buried hydrophobic surface, but the beta-sheet of native Arc is not formed. Moreover, relatively little side chain information appears to be used in the transition state, suggesting that tight packing of the hydrophobic core and optimization of hydrogen-bond geometry are events that occur later in folding.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. O. Huising, J. M. Vaughan, S. H. Shah, K. L. Grillot, C. J. Donaldson, J. Rivier, G. Flik, and W. W. Vale
Residues of Corticotropin Releasing Factor-binding Protein (CRF-BP) That Selectively Abrogate Binding to CRF but Not to Urocortin 1
J. Biol. Chem., April 4, 2008; 283(14): 8902 - 8912.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
N. A.J. van Nuland, C. M. Dobson, and L. Regan
Characterization of folding the four-helix bundle protein Rop by real-time NMR
Protein Eng. Des. Sel., March 1, 2008; 21(3): 165 - 170.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
S. Dalal, D. Canet, S. E. Kaiser, C. M. Dobson, and L. Regan
Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins
Protein Eng. Des. Sel., March 1, 2008; 21(3): 197 - 206.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. J. Behe and D. W. Snoke
Simulating evolution by gene duplication of protein features that require multiple amino acid residues
Protein Sci., October 22, 2004; 13(10): 2651 - 2664.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
D. D. Ojennus, S. E. Lehto, and D. S. Wuttke
Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments
Protein Sci., January 1, 2003; 12(1): 44 - 55.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J.-L. Chen, L.-C. Tsai, T.-N. Wen, J.-B. Tang, H. S. Yuan, and L.-F. Shyur
Directed Mutagenesis of Specific Active Site Residues on Fibrobacter succinogenes 1,3-1,4-beta -D-Glucanase Significantly Affects Catalysis and Enzyme Structural Stability
J. Biol. Chem., May 18, 2001; 276(21): 17895 - 17901.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by The Federation of American Societies for Experimental Biology.