Amino Acid Selective 13C Labeling and 13C Scrambling Profile Analysis of Protein α and Side-Chain Carbons in Escherichia coli Utilized for Protein Nuclear Magnetic Resonance
Author:
Affiliation:
1. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
2. Graduate School of Engineering Science, Yokohama National University, 79-5 Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan
Funder
Ministry of Education, Culture, Sports, Science and Technology
Core Research for Evolutional Science and Technology
Japan Agency for Medical Research and Development
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00182
Reference61 articles.
1. THE USE OF 2H, 13C, 15N MULTIDIMENSIONAL NMR GTO STUDY THE STRUCTURE AND DYNAMICS OF PROTEINS
2. [3] Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
3. Amino Acid Selective Labeling and Unlabeling for Protein Resonance Assignments
4. Genetic tools for selective labeling of proteins with ?-15N-amino acids
5. Amino acid selective unlabeling for sequence specific resonance assignments in proteins
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