Journal Article

PreJuSER-49010

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural and dynamical features contributing to thermostability in alpha-amylases

Fitter, J.FZJ*

2005
Birkhäuser Basel

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Please use a persistent id in citations: doi:10.1007/s00018-005-5079-2

Abstract: In recent years an increasing number of studies on thermophilic and hyperthermophilic proteins aiming to elucidate determinants of protein thermostability have yielded valuable insights about the relevant mechanisms. In particular, comparison of homologous enzymes with different thermostabilities (isolated from psychrophilic, mesophilic, thermophilic and hyperthermophilic organisms) offers a unique opportunity to determine the strategies of thermal adaptation. In this respect, the medium-sized amylolytic enzyme alpha-amylase is a well-established representative. Various studies on alpha-amylases with very different thermostabilities (melting temperature T(m) = 40-110 degrees C) report structural and dynamical features as well as thermodynamical properties which are supposed to play key roles in thermal adaptation. Here, results from selected homologous alpha-amylases are presented and discussed with respect to some new and recently proposed strategies to achieve thermostability.

Keyword(s): Enzyme Stability (MeSH) ; Protein Conformation (MeSH) ; Protein Folding (MeSH) ; Temperature (MeSH) ; alpha-Amylases: chemistry (MeSH) ; alpha-Amylases ; J ; protein stability (auto) ; protein unfolding (auto) ; protein dynamics (auto) ; thermal adaptation (auto) ; unfolded states (auto) ; conformational entropy (auto)

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologische Strukturforschung (IBI-2)

Research Program(s):

1. Neurowissenschaften (L01)

Appears in the scientific report 2005

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