Literature DB >> 9697297

Internal motions of native lysozyme are more organized than those of mutants: a principal component analysis of molecular dynamics data.

R Laatikainen, J Saarela, K Tuppurainen, T Hassinen.   

Abstract

Principal component analysis (PCA) of molecular dynamics simulations of hen egg white lysozyme and its mutants indicate that even small changes in the amino acid sequence alter considerably the internal molecular motions and that the internal motions are more organized in the native enzyme than in the mutants.

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Year:  1998        PMID: 9697297     DOI: 10.1016/s0301-4622(98)00141-0

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  Ligand intramolecular motions in ligand-protein interaction: ALPHA, a novel dynamic descriptor and a QSAR study with extended steroid benchmark dataset.

Authors:  Kari Tuppurainen; Marja Viisas; Mikael Peräkylä; Reino Laatikainen
Journal:  J Comput Aided Mol Des       Date:  2004-03       Impact factor: 3.686

  1 in total

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