Activity-stability relationships in extremophilic enzymes.
TLDR
The shape of the funnel bottom, which depicts the stability of the native state ensemble, also accounts for the thermodynamic parameters of activation that characterize these extremophilic enzymes, therefore providing a rational basis for stability-activity relationships in protein adaptation to extreme temperatures.About:
This article is published in Journal of Biological Chemistry.The article was published on 2003-03-07 and is currently open access. It has received 441 citations till now. The article focuses on the topics: Folding funnel & Cooperativity.read more
Citations
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疟原虫var基因转换速率变化导致抗原变异[英]／Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A
TL;DR: PfPMP1）与感染红细胞、树突状组胞以及胎盘的单个或多个受体作用，在黏附及免疫逃避中起关键的作�ly.
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Psychrophilic enzymes: Hot topics in cold adaptation
Georges Feller,Charles Gerday +1 more
TL;DR: The ability to thrive at temperatures that are close to, or below, the freezing point of water requires a vast array of adaptations to maintain the metabolic rates and sustained growth compatible with life in these severe environmental conditions.
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Cold-adapted enzymes.
TL;DR: This review addresses the structure, function, and stability of cold-adapted enzymes, highlighting the challenges for immediate and future consideration.
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Directed evolution of industrial enzymes: an update
Joel R. Cherry,Ana Fidantsef +1 more
TL;DR: The use of enzymes in industrial processes can often eliminate the use of high temperatures, organic solvents and extremes of pH, while at the same time offering increased reaction specificity, product purity and reduced environmental impact.
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Psychrophilic microorganisms: challenges for life
TL;DR: The ability of psychrophiles to survive and proliferate at low temperatures implies that they have overcome key barriers inherent to permanently cold environments, and the current knowledge of these adaptations as gained from extensive biochemical and biophysical studies and also from genomics and proteomics is discussed.
References
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Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
From Levinthal to pathways to funnels
Ken A. Dill,Hue Sun Chan +1 more
TL;DR: The general energy landscape picture provides a conceptual framework for understanding both two-state and multi-state folding kinetics and hopes to learn much more about the real shapes of protein folding landscapes.
Book ChapterDOI
Determination and analysis of urea and guanidine hydrochloride denaturation curves.
Book ChapterDOI
Stability of Proteins Small Globular Proteins
TL;DR: The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system, and the temperature-induced changes in protein, denaturational and predenaturational changes inprotein, thermodynamics of protein unfolding, and thermodynamic properties of protein.
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