A Nuclear Magnetic Resonance Method for Probing Molecular Influences of Substrate Loading in Nonribosomal Peptide Synthetase Carrier Proteins
Author:
Affiliation:
1. Department of Biophysics & Biophysical Chemistry, Johns Hopkins University School of Medicine, 701 Hunterian Building, 725 North Wolfe Street, Baltimore, Maryland 21205, United States
Funder
American Heart Association
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi501433r
Reference22 articles.
1. Polyketide and Nonribosomal Peptide Antibiotics: Modularity and Versatility
2. Rational Design of Peptide Antibiotics by Targeted Replacement of Bacterial and Fungal Domains
3. Dynamic thiolation–thioesterase structure of a non-ribosomal peptide synthetase
4. Crystal Structure of the Termination Module of a Nonribosomal Peptide Synthetase
5. Conformational Switches Modulate Protein Interactions in Peptide Antibiotic Synthetases
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