Document Detail


Integral membrane proteins and bilayer proteomics.
MedLine Citation:
PMID:  23301778     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Integral membrane proteins reside within the bilayer membranes that surround cells and organelles, playing critical roles in movement of molecules across them and the transduction of energy and signals. While their extreme amphipathicity presents technical challenges, biological mass spectrometry has been applied to all aspects of membrane protein chemistry and biology, including analysis of primary, secondary, tertiary, and quaternary structures as well as the dynamics that accompany functional cycles and catalysis.
Authors:
Julian P Whitelegge
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2013-02-19
Journal Detail:
Title:  Analytical chemistry     Volume:  85     ISSN:  1520-6882     ISO Abbreviation:  Anal. Chem.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-05     Completed Date:  2013-11-19     Revised Date:  2014-03-07    
Medline Journal Info:
Nlm Unique ID:  0370536     Medline TA:  Anal Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2558-68     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cell Membrane / metabolism
Lipid Bilayers / metabolism*
Mass Spectrometry
Membrane Proteins / chemistry,  metabolism*
Molecular Sequence Data
Protein Processing, Post-Translational
Proteomics / methods*
Grant Support
ID/Acronym/Agency:
GM088499/GM/NIGMS NIH HHS; P50 GM088499/GM/NIGMS NIH HHS; S10 RR023045/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Lipid Bilayers; 0/Membrane Proteins
Comments/Corrections

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