Literature DB >> 429093

An analysis of side-chain conformation in proteins.

T N Bhat, V Sasisekharan, M Vijayan.   

Abstract

The crystal structures of a number of globular proteins are currently available. An analysis of the distribution of side-chains among different allowed conformations in these proteins has been carried out. The observed conformations of individual residues are discussed on the basis of well-known stereochemical criteria. The population distribution of side-chains in different allowed regions in conformational space can be explained largely on the basis of simple steric considerations. In addition to examining the conformational behaviour of individual residues, some population distributions of conformational angles of general interest involving groups of residues have also been analyzed.

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Year:  1979        PMID: 429093     DOI: 10.1111/j.1399-3011.1979.tb01866.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  18 in total

1.  Flexibility in crystalline insulins.

Authors:  J Badger
Journal:  Biophys J       Date:  1992-03       Impact factor: 4.033

2.  Molecular modelling prediction of ligand binding site flexibility.

Authors:  Ami Yi-Ching Yang; Per Källblad; Ricardo L Mancera
Journal:  J Comput Aided Mol Des       Date:  2004-04       Impact factor: 3.686

3.  Side-chain conformational space analysis (SCSA): a multi conformation-based QSAR approach for modeling and prediction of protein-peptide binding affinities.

Authors:  Peng Zhou; Xiang Chen; Zhicai Shang
Journal:  J Comput Aided Mol Des       Date:  2008-10-08       Impact factor: 3.686

4.  Asparagine and glutamine rotamers: B-factor cutoff and correction of amide flips yield distinct clustering.

Authors:  S C Lovell; J M Word; J S Richardson; D C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  1999-01-19       Impact factor: 11.205

5.  High-resolution structure and dynamic implications for a double-helical gramicidin A conformer.

Authors:  S M Pascal; T A Cross
Journal:  J Biomol NMR       Date:  1993-09       Impact factor: 2.835

6.  Bayesian statistical analysis of protein side-chain rotamer preferences.

Authors:  R L Dunbrack; F E Cohen
Journal:  Protein Sci       Date:  1997-08       Impact factor: 6.725

7.  Assessment of protein side-chain conformation prediction methods in different residue environments.

Authors:  Lenna X Peterson; Xuejiao Kang; Daisuke Kihara
Journal:  Proteins       Date:  2014-03-31

8.  Probing alpha-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation.

Authors:  K J Willis; W Neugebauer; M Sikorska; A G Szabo
Journal:  Biophys J       Date:  1994-05       Impact factor: 4.033

9.  Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins.

Authors:  R W Woody
Journal:  Eur Biophys J       Date:  1994       Impact factor: 1.733

10.  X-ray diffraction studies of enkephalins. Crystal structure of [(4'-bromo) Phe4,Leu5]enkephalin.

Authors:  T Ishida; M Kenmotsu; Y Mino; M Inoue; T Fujiwara; K Tomita; T Kimura; S Sakakibara
Journal:  Biochem J       Date:  1984-03-15       Impact factor: 3.857

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