Work

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

Year: 2021

Type: article

Abstract: occupancy across the four monomers of the tetrameric enzyme. The structure of the fully occupied monomers was compared to those with partial cofactor occupancy, identifying regions of difference that may account for the increased thermal stability.

Source: RSC Advances

DOI: 10.1039/d0ra10119b

Authors: Astrid M. Perez, Jacob A. Wolfe, Janse T. Schermerhorn, Yiwen Qian, Bekim A. Cela, Cody R. Kalinowski, Garrett E. Largoza, Peter A. Fields, Gabriel S. Brandt

Institution: Franklin & Marshall College

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: gold

Estimated APC paid: $1,042

Funders: National Science Foundation, Franklin and Marshall College, Argonne National Laboratory

Award: RUI: Biochemical adaptation to temperature in the coral-dinoflagellate symbiosis

OpenAlex ID: W3133872840

FWCI: 0.076

Cites: 57

Cited by: 3

Related to: 10