Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy.
J Am Chem Soc
; 131(1): 170-6, 2009 Jan 14.
Article
en En
| MEDLINE
| ID: mdl-19063626
ABSTRACT
We show that water-edited solid-state NMR spectroscopy allows for probing global protein conformation and residue-specific solvent accessibility in a lipid bilayer environment. The transfer dynamics can be well described by a general time constant, irrespective of protein topology and lipid environment. This approach was used to follow structural changes in response to protein function in the chimeric potassium channel KcsA-Kv1.3. Data obtained as a function of pH link earlier biochemical data to changes in protein structure in a functional bilayer setting.
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1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
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Proteínas de Unión al Calcio
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Canales de Potasio
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Resonancia Magnética Nuclear Biomolecular
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Halorrodopsinas
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Rodopsinas Sensoriales
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Membrana Dobles de Lípidos
Idioma:
En
Revista:
J Am Chem Soc
Año:
2009
Tipo del documento:
Article
País de afiliación:
Países Bajos