Dynamic structure of subtilisin-eglin c complex studied by normal mode analysis
作者： Hisashi Ishida , Yasumasa Jochi , Akinori Kidera
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<324::AID-PROT8>3.0.CO;2-H
关键词: Subtilisin 、 Hydrophobic effect 、 Amplitude 、 Positive correlation 、 Conformational entropy 、 Normal mode 、 Chemistry 、 Entropy (order and disorder) 、 Crystallography 、 Chemical physics 、 Molecule 、 Biochemistry 、 Molecular biology 、 Structural biology
摘要: Normal mode analysis of subtilisin-eglin c complex was performed to investigate the dynamics at interface between enzyme and inhibitor. The internal motions calculated from normal modes were divided into three parts: changing shape each molecule, external rigid-body their mutual dispositions, coupling motions. From results analysis, following characteristic features found in regions: 1) negative correlation within 2) positive two molecules. former decreases apparent amplitudes interface. latter minimizes interference individual These dynamic characteristics allow inhibitor move as freely possible. This finding suggests that experimental evidence large entropy gain on binding should be attributed not only strong hydrophobic interactions, but also structure complex, which is minimize an unavoidable loss conformational binding. Proteins 32:324–333, 1998. © 1998 Wiley-Liss, Inc.
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