NMR reveals novel mechanisms of protein activity regulation

NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site‐resolved information about th...

Full description

Saved in:
Bibliographic Details
Published in:Protein science 2011-05, Vol.20 (5), p.773-782
Main Author: Kalodimos, Charalampos G.
Format: Article
Language:English
Subjects:
allosteric interactions
Allosteric Regulation
Animals
autoinhibition
Humans
Magnetic Resonance Spectroscopy - methods
Models, Chemical
Models, Molecular
NMR
Nuclear magnetic resonance
Protein Binding
Protein Conformation
protein function
protein regulation
Protein Structure, Tertiary
Proteins - chemistry
Proteins - metabolism
Review
Spectrum analysis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site‐resolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.614