Affordable Access

NMR of membrane-associated peptides and proteins.

Authors
  • Wang, Guangshun
Type
Published Article
Journal
Current Protein and Peptide Science
Publisher
Bentham Science
Publication Date
Feb 01, 2008
Volume
9
Issue
1
Pages
50–69
Identifiers
PMID: 18336323
Source
Medline
License
Unknown

Abstract

In living cells, membrane proteins are essential to signal transduction, nutrient use, and energy exchange between the cell and environment. Due to challenges in protein expression, purification and crystallization, deposition of membrane protein structures in the Protein Data Bank lags far behind existing structures for soluble proteins. This review describes recent advances in solution NMR allowing the study of a select set of peripheral and integral membrane proteins. Surface-binding proteins discussed include amphitropic proteins, antimicrobial and anticancer peptides, the HIV-1 gp41 peptides, human alpha-synuclein and apolipoproteins. Also discussed are transmembrane proteins including bacterial outer membrane beta-barrel proteins and oligomeric alpha-helical proteins. These structural studies are possible due to solubilization of the proteins in membrane-mimetic constructs such as detergent micelles and bicelles. In addition to protein dynamics, protein-lipid interactions such as those between arginines and phosphatidylglycerols have been detected directly by NMR. These examples illustrate the unique role solution NMR spectroscopy plays in structural biology of membrane proteins.

Report this publication

Statistics

Seen <100 times