Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coral Acropora millepora-Reference-Cited by-同舟云学术

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Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coral Acropora millepora

Published:2021 Issue:17 Volume:11 Page:10364-10374
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Perez Astrid M.¹²³⁴,Wolfe Jacob A.¹²³⁴^ORCID,Schermerhorn Janse T.¹²³⁴⁵,Qian Yiwen¹²³⁴,Cela Bekim A.⁵²³⁴,Kalinowski Cody R.⁵²³⁴,Largoza Garrett E.⁵²³⁴,Fields Peter A.⁵²³⁴^ORCID,Brandt Gabriel S.¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Franklin & Marshall College

3. Lancaster

4. USA

5. Department of Biology

Abstract

The thermal stability of a critical coral metabolic enzyme increases significantly in the presence of its cofactor. X-ray crystallography identifies the protein backbone changes associated with cofactor occupancy.

Funder

Directorate for Biological Sciences National Science Foundation

Franklin and Marshall College

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/RA/D0RA10119B

Reference53 articles.

1. Stability effects of mutations and protein evolvability

2. Adaptation of enzymes to temperature: searching for basic “strategies”

3. Review: Protein function at thermal extremes: balancing stability and flexibility

4. Living in the Now: Physiological Mechanisms to Tolerate a Rapidly Changing Environment

5. Protein stability imposes limits on organism complexity and speed of molecular evolution

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