Hayden Baer

College of Agriculture and Life Sciences

2021 journal article

Structure, Function, and Thermal Adaptation of the Biotin Carboxylase Domain Dimer from Hydrogenobacter thermophilus 2-Oxoglutarate Carboxylase

BIOCHEMISTRY, 60(4), 324–345.

MeSH headings : Bacteria / enzymology; Bacterial Proteins / chemistry; Carbon-Nitrogen Ligases / chemistry; Crystallography, X-Ray; Enzyme Stability; Hot Temperature; Protein Domains; Structure-Activity Relationship
TL;DR: Structural data reveal that the OGC BC dimer comprises a "wet" dimerization interface that is dominated by hydrophilic interactions and structural water molecules common to all BC domains and likely facilitates the conformational changes associated with the catalytic cycle. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, ORCID, NC State University Libraries
Added: January 20, 2021

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.