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1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide

Overview of attention for article published in Biomolecular NMR Assignments, June 2012
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Title
1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide
Published in
Biomolecular NMR Assignments, June 2012
DOI 10.1007/s12104-012-9407-9
Pubmed ID
Authors

Piotr Wysoczanski, Robert J. Mart, E. Joel Loveridge, Christopher Williams, Sara B.-M. Whittaker, Matthew P. Crump, Rudolf K. Allemann

Abstract

Here we report the (1)H, (13)C and (15)N resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 13 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 13 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 31%
Student > Master 3 23%
Researcher 2 15%
Lecturer 1 8%
Student > Bachelor 1 8%
Other 0 0%
Unknown 2 15%
Readers by discipline Count As %
Chemistry 5 38%
Agricultural and Biological Sciences 3 23%
Pharmacology, Toxicology and Pharmaceutical Science 1 8%
Medicine and Dentistry 1 8%
Environmental Science 1 8%
Other 0 0%
Unknown 2 15%