Measurement of methyl axis orientations in invisible, excited states of proteins by relaxation dispersion NMR spectroscopy.
Few detailed studies of transiently populated conformations of biological molecules have emerged despite the fact that such states are often important to processes such as protein folding, enzyme catalysis, molecular recognition and binding. A major limitation has been the lack of experimental tools...
Asıl Yazarlar: | Baldwin, A, Hansen, D, Vallurupalli, P, Kay, L |
---|---|
Materyal Türü: | Journal article |
Dil: | English |
Baskı/Yayın Bilgisi: |
2009
|
Benzer Materyaller
-
NMR spectroscopy brings invisible protein states into focus.
Yazar:: Baldwin, A, ve diğerleri
Baskı/Yayın Bilgisi: (2009) -
13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
Yazar:: Baldwin, A, ve diğerleri
Baskı/Yayın Bilgisi: (2010) -
Relaxing the Shackles: The Invisible Pendulum.
Yazar:: Stewart, F
Baskı/Yayın Bilgisi: (2009) -
Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy.
Yazar:: Baldwin, A, ve diğerleri
Baskı/Yayın Bilgisi: (2012) -
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.
Yazar:: Baldwin, A, ve diğerleri
Baskı/Yayın Bilgisi: (2012)