Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better

Sébastien F. Poget, Mark E. Girvin

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

Considerable progress has been made recently on solution NMR studies of multi-transmembrane helix membrane protein systems of increasing size. Careful correlation of structure with function has validated the physiological relevance of these studies in detergent micelles. However, larger micelle and bicelle systems are sometimes required to stabilize the active forms of dynamic membrane proteins, such as the bacterial small multidrug resistance transporters. Even in these systems with aggregate molecular weights well over 100 kDa, solution NMR structural studies are feasible-but challenging.

Original languageEnglish (US)
Pages (from-to)3098-3106
Number of pages9
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1768
Issue number12
DOIs
StatePublished - Dec 2007

Fingerprint

Micelles
Membrane Proteins
Nuclear magnetic resonance
Multiple Drug Resistance
Detergents
Molecular Weight
Molecular weight

Keywords

  • Bicelle
  • Micelle
  • Multidrug resistance
  • Smr
  • Structure

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Biophysics

Cite this

Solution NMR of membrane proteins in bilayer mimics : Small is beautiful, but sometimes bigger is better. / Poget, Sébastien F.; Girvin, Mark E.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1768, No. 12, 12.2007, p. 3098-3106.

Research output: Contribution to journalArticle

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