Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis

1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus... Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis

Loading next page...
 
/lp/springer-journals/1h-13c-and-15n-chemical-shift-assignments-for-an-intracellular-Q90fiHLtc5

References (11)

Publisher
Springer Journals
Copyright
Copyright © 2012 by Springer Science+Business Media B.V.
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-012-9392-z
pmid
22585087
Publisher site
See Article on Publisher Site

Abstract

Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: May 15, 2012

There are no references for this article.