Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Berezovsky, I. N.
Right arrow Articles by Trifonov, E. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Berezovsky, I. N.
Right arrow Articles by Trifonov, E. N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 14, No. 6, 403-407, June 2001
© 2001 Oxford University Press

Loop fold nature of globular proteins

Igor N. Berezovsky1, and Edward N. Trifonov

Department of Structural Biology, The Weizmann Institute of Science, P.O.B. 26, Rehovot 76100, Israel

Protein chains make numerous returns in globules, thus forming loops, closed by tight residue-to-residue contacts—closed loops. Previous statistical analysis of the sizes and locations of the closed loops in all major protein folds revealed that the loops have an almost standard contour length of 25–30 amino acid residues and follow one after another along the chain. In this work the closed loops of the major folds are presented in three dimensions. A special image filtering procedure is introduced that allows one to visualize the standard size closed loops for the first time. The loop positions along the sequences are verified by detection of loop-end clusters.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
I. N. Berezovsky
Discrete structure of van der Waals domains in globular proteins
Protein Eng. Des. Sel., March 1, 2003; 16(3): 161 - 167.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
I. N. Berezovsky, V. M. Kirzhner, A. Kirzhner, V. R. Rosenfeld, and E. N. Trifonov
Closed loops: persistence of the protein chain returns
Protein Eng. Des. Sel., December 1, 2002; 15(12): 955 - 957.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.