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Interaction and conformational dynamics of membrane‐spanning protein helices
Author(s) -
Langosch Dieter,
Arkin Isaiah T.
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.154
Subject(s) - transmembrane protein , biophysics , transmembrane domain , protein structure , membrane protein , chemistry , function (biology) , conformational change , biology , membrane , biochemistry , microbiology and biotechnology , receptor
Within 1 or 2 decades, the reputation of membrane‐spanning α‐helices has changed dramatically. Once mostly regarded as dull membrane anchors, transmembrane domains are now recognized as major instigators of protein–protein interaction. These interactions may be of exquisite specificity in mediating assembly of stable membrane protein complexes from cognate subunits. Further, they can be reversible and regulatable by external factors to allow for dynamic changes of protein conformation in biological function. Finally, these helices are increasingly regarded as dynamic domains. These domains can move relative to each other in different functional protein conformations. In addition, small‐scale backbone fluctuations may affect their function and their impact on surrounding lipid shells. Elucidating the ways by which these intricate structural features are encoded by the amino acid sequences will be a fascinating subject of research for years to come.