Umbrella Sampling Simulations of Biotin Carboxylase: Is a Structure with an Open ATP Grasp Domain Stable in Solution?
Author:
Affiliation:
1. Departments of Mechanical Engineering and Biological Sciences, Louisiana State University, Baton Rouge, Louisiana, 70803, USA
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp810650q
Reference40 articles.
1. Is Dimerization Required for the Catalytic Activity of Bacterial Biotin Carboxylase?
2. Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding
3. Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase
4. Molecular Dynamics Simulations of Biotin Carboxylase
5. The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase
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