Literature DB >> 11477219

Loop fold nature of globular proteins.

I N Berezovsky1, E N Trifonov.   

Abstract

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.

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Year:  2001        PMID: 11477219     DOI: 10.1093/protein/14.6.403

Source DB:  PubMed          Journal:  Protein Eng        ISSN: 0269-2139


  10 in total

1.  CONTSOR--a new knowledge-based fold recognition potential, based on side chain orientation and contacts between residue terminal groups.

Authors:  Boris Vishnepolsky; Malak Pirtskhalava
Journal:  Protein Sci       Date:  2011-11-23       Impact factor: 6.725

2.  A new method to improve network topological similarity search: applied to fold recognition.

Authors:  John Lhota; Ruth Hauptman; Thomas Hart; Clara Ng; Lei Xie
Journal:  Bioinformatics       Date:  2015-02-25       Impact factor: 6.937

Review 3.  The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.

Authors:  Tomer Orevi; Gil Rahamim; Gershon Hazan; Dan Amir; Elisha Haas
Journal:  Biophys Rev       Date:  2013-04-12

4.  Functional states of homooligomers: insights from the evolution of glycosyltransferases.

Authors:  Kosuke Hashimoto; Thomas Madej; Stephen H Bryant; Anna R Panchenko
Journal:  J Mol Biol       Date:  2010-04-08       Impact factor: 5.469

5.  Flowering buds of globular proteins: transpiring simplicity of protein organization.

Authors:  Igor N Berezovsky; Edward N Trifonov
Journal:  Comp Funct Genomics       Date:  2002

6.  Evidence for the emergence of β-trefoils by 'Peptide Budding' from an IgG-like β-sandwich.

Authors:  Liam M Longo; Rachel Kolodny; Shawn E McGlynn
Journal:  PLoS Comput Biol       Date:  2022-02-14       Impact factor: 4.475

7.  Predicting exon criticality from protein sequence.

Authors:  Jigar Desai; Christopher Francis; Kenneth Longo; Andrew Hoss
Journal:  Nucleic Acids Res       Date:  2022-04-08       Impact factor: 16.971

8.  Random amino acid mutations and protein misfolding lead to Shannon limit in sequence-structure communication.

Authors:  Andreas Martin Lisewski
Journal:  PLoS One       Date:  2008-09-01       Impact factor: 3.240

9.  Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures.

Authors:  Alberto Pascual-García; David Abia; Angel R Ortiz; Ugo Bastolla
Journal:  PLoS Comput Biol       Date:  2009-03-27       Impact factor: 4.475

10.  Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.

Authors:  Jose Sergio Hleap; Edward Susko; Christian Blouin
Journal:  BMC Struct Biol       Date:  2013-10-16
  10 in total

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