Solution NMR Studies of a 42 KDa Escherichia Coli Maltose Binding Protein/β-Cyclodextrin Complex: Chemical Shift Assignments and Analysis-Reference-Cited by-同舟云学术

Solution NMR Studies of a 42 KDa Escherichia Coli Maltose Binding Protein/β-Cyclodextrin Complex: Chemical Shift Assignments and Analysis

Published:1998-11-01 Issue:45 Volume:120 Page:11738-11748
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Gardner Kevin H.¹,Zhang Xiaochen¹,Gehring Kalle¹,Kay Lewis E.¹

Affiliation:

1. Contribution from the: Protein Engineering Network Centres of Excellence and Departments of Medical Genetics and Microbiology, Biochemistry, and Chemistry, University of Toronto, Toronto ON M5S 1A8 Canada, and Department of Biochemistry and Montreal Joint Centre for Structural Biology, McGill University, Montreal QC H3G 1Y6 Canada

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja982019w

Reference55 articles.

1. NMR with Proteins and Nucleic Acids

2. 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus

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