Format

Send to

Choose Destination
Biochim Biophys Acta. 2013 Jun;1834(6):1202-9. doi: 10.1016/j.bbapap.2012.10.009. Epub 2012 Oct 22.

Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.

Author information

1
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0378, USA.

Abstract

Amide hydrogen/deuterium exchange detected by mass spectrometry (HXMS) is seeing wider use for the identification of intrinsically disordered parts of proteins. In this review, we discuss examples of how discovery of intrinsically disordered regions and their removal can aid in structure determination, biopharmaceutical quality control, the characterization of how post-translational modifications affect weak structuring of disordered regions, the study of coupled folding and binding, and the characterization of amyloid formation. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.

PMID:
23099262
PMCID:
PMC3600394
DOI:
10.1016/j.bbapap.2012.10.009
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center