Dynamics in Thermotoga neapolitana Adenylate Kinase: 15N Relaxation and Hydrogen−Deuterium Exchange Studies of a Hyperthermophilic Enzyme Highly Active at 30 °C-Reference-Cited by-同舟云学术

Dynamics in Thermotoga neapolitana Adenylate Kinase: 15N Relaxation and Hydrogen−Deuterium Exchange Studies of a Hyperthermophilic Enzyme Highly Active at 30 °C

Published:2009-02-16 Issue:12 Volume:48 Page:2723-2739
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Krishnamurthy Harini¹,Munro Kim¹,Yan Honggao¹,Vieille Claire¹

Affiliation:

1. Program in Cell and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, Queen’s Protein Function Discovery Facility, Queen’s University, Kingston, Ontario, Canada K7L-3N6, and Department of Biochemistry and Molecular Biology and Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan 48824

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi802001w

Reference68 articles.

1. Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability

2. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima

3. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

4. Activity-Stability Relationships in Extremophilic Enzymes

5. Temperature Adaptation of Enzymes: Biological Optimization Through Structure-Function Compromises

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