Folding Mechanism of an Extremely Thermostable (βα)8-Barrel Enzyme: A High Kinetic Barrier Protects the Protein from Denaturation-Reference-Cited by-同舟云学术

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Folding Mechanism of an Extremely Thermostable (βα)8-Barrel Enzyme: A High Kinetic Barrier Protects the Protein from Denaturation

Published:2012-04-11 Issue:16 Volume:51 Page:3420-3432
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Carstensen Linn¹,Zoldák Gabriel²,Schmid Franz-Xaver³,Sterner Reinhard¹

Affiliation:

1. Universität Regensburg, Institut für Biophysik und physikalische Biochemie, Universitätsstrasse 31, D-93053 Regensburg, Germany

2. Physik Department E22, Technische Universität München, D-85748 Garching, Germany

3. Universität Bayreuth, Laboratorium für Biochemie, D-95440 Bayreuth, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300189f

Reference63 articles.

1. The origin of modern metabolic networks inferred from phylogenomic analysis of protein architecture

2. The TIM-barrel fold: a versatile framework for efficient enzymes

3. Catalytic Versatility, Stability, and Evolution of the (βα)8-Barrel Enzyme Fold

4. One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and Functions

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