Protein dynamics from nuclear magnetic relaxation
نویسندگان
چکیده
منابع مشابه
Nuclear Magnetic Relaxation Dispersion in Protein Solutions
Bovine and human B erythrocyte carbonic anhydrases substituted with Co2+ cause an enhancement of the nuclear magnetic relaxation rate of solvent water protons (T1-l) at high pH that is decreased by the addition of carbonic anhydrase inhibitors such as azide and Ethoxzolamide. The part of T1-1 which can be inhibited by Ethoxzolamide is due to exchangeable protons located at the active site of th...
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Results are presented for the relaxation of the nuclear magnetization via quadrupolar interactions caused by the dynamics of point-like lattice defects in cubic solids. For systems with nuclear spins I = 3/2, several aspects of the lineshape function of the absorption signal are considered. The treatment includes the transition to the rigid lattice case, the presence of additional static quadru...
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Antimony nuclear quadrupole resonance frequencies in (NH 4 ) 6 Sb 4 (S0 4 ) 3 F 1 2 crystals were measured as a function of temperature, and no evidence of phase transition was detected between 77 K and room temperature. However, the resonance frequencies do not follow the Bayer type exactly. Such an anomaly is attributed to the effect of rotation of ammonium ions which form hydrogen bonds of t...
متن کاملSlow internal protein dynamics from water (1)H magnetic relaxation dispersion.
To probe internal motions in proteins on the 10(-8)-10(-5) s time scale by NMR relaxation, it is necessary to eliminate protein tumbling. Here, we examine to what extent magnetic relaxation dispersion (MRD) experiments on the water (1)H resonance report on protein motions in this time window. We also perform a critical test of two physically distinct mechanisms that have been proposed to explai...
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ژورنال
عنوان ژورنال: Chemical Society Reviews
سال: 2016
ISSN: 0306-0012,1460-4744
DOI: 10.1039/c5cs00832h