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


     

Published online before print February 6, 2004, 10.1110/ps.03503304
Protein Science (2004), 13:633-639. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.03503304v1
13/3/633    most recent
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 Fitzkee, N. C.
Right arrow Articles by Rose, G. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fitzkee, N. C.
Right arrow Articles by Rose, G. 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?

Steric restrictions in protein folding: An {alpha}-helix cannot be followed by a contiguous {beta}-strand

Nicholas C. Fitzkee and George D. Rose

T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA

(RECEIVED October 31, 2003; FINAL REVISION December 2, 2003; ACCEPTED December 3, 2003)



Abstract

Using only hard-sphere repulsion, we investigated short polyalanyl chains for the presence of sterically imposed conformational constraints beyond the dipeptide level. We found that a central residue in a helical peptide cannot adopt dihedral angles from strand regions without encountering a steric collision. Consequently, an {alpha}-helical segment followed by a {beta}-strand segment must be connected by an intervening linker. This restriction was validated both by simulations and by seeking violations within proteins of known structure. In fact, no violations were found within an extensive database of high-resolution X-ray structures. Nature’s exclusion of {alpha}-{beta} hybrid segments, fashioned from an {alpha}-helix adjoined to a {beta}-strand, is built into proteins at the covalent level. This straightforward conformational constraint has far-reaching consequences in organizing unfolded proteins and limiting the number of possible protein domains.

Keywords: protein folding; unfolded protein; protein secondary structure; Ramachandran plot

Reprint requests to: George D. Rose, T.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA; e-mail: grose{at}jhu.edu; fax: (410) 516-4118.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03503304.


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
 Protein Sci.Home page
L. L. Perskie, T. O. Street, and G. D. Rose
Structures, basins, and energies: A deconstruction of the Protein Coil Library
Protein Sci., July 1, 2008; 17(7): 1151 - 1161.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Gong and G. D. Rose
Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model
PNAS, March 4, 2008; 105(9): 3321 - 3326.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
T. O. Street, N. C. Fitzkee, L. L. Perskie, and G. D. Rose
Physical-chemical determinants of turn conformations in globular proteins
Protein Sci., August 1, 2007; 16(8): 1720 - 1727.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
G. D. Rose, P. J. Fleming, J. R. Banavar, and A. Maritan
A backbone-based theory of protein folding
PNAS, November 7, 2006; 103(45): 16623 - 16633.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Gong, P. J. Fleming, and G. D. Rose
From The Cover: Building native protein conformation from highly approximate backbone torsion angles
PNAS, November 8, 2005; 102(45): 16227 - 16232.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
E. V. Kuzmenkina, C. D. Heyes, and G. U. Nienhaus
Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions
PNAS, October 25, 2005; 102(43): 15471 - 15476.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. C. Fitzkee and G. D. Rose
Reassessing random-coil statistics in unfolded proteins
PNAS, August 24, 2004; 101(34): 12497 - 12502.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by The Protein Society.