Riding the wave: structural and energetic principles of helical membrane proteins

Genome sequencing efforts have revealed that perhaps as many as 20–40% of open reading frames in complex organisms may encode proteins containing at least one helical transmembrane segment. Contrasting with this approaching tidal wave of helical membrane proteins is the fact that our understanding o...

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Bibliographic Details
Published in:Current Opinion in Biotechnology 2000-02, Vol.11 (1), p.67-71
Main Author: Fleming, Karen G
Format: Article
Language:English
Subjects:
Animals
Crystallization
Crystallography, X-Ray
Energetics
GTP-Binding Proteins - metabolism
Humans
Mass Spectrometry
Membrane protein
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - isolation & purification
Membrane Proteins - metabolism
Protein Engineering
Protein structure
Protein Structure, Secondary
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - genetics
Receptors, Cell Surface - isolation & purification
Receptors, Cell Surface - metabolism
Structure-Activity Relationship
Thermodynamics
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Summary:Genome sequencing efforts have revealed that perhaps as many as 20–40% of open reading frames in complex organisms may encode proteins containing at least one helical transmembrane segment. Contrasting with this approaching tidal wave of helical membrane proteins is the fact that our understanding of the sequence–structure–function relationships for membrane proteins lags far behind that of soluble proteins. This looming reality emphasizes the tremendous biochemical and structural work that remains to be done on helical membrane proteins in order to elucidate the structural and energetic principles that specify and stabilize their folds, which define their functions. These facts are not lost on the pharmaceutical industry, where successful therapeutics and major discovery efforts are targeting membrane proteins.
ISSN:0958-1669
1879-0429
DOI:10.1016/S0958-1669(99)00056-7