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PDBsum entry 1u06
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Structural protein
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PDB id
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1u06
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References listed in PDB file
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Key reference
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Title
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Detection of dynamic water molecules in a microcrystalline sample of the sh3 domain of alpha-Spectrin by mas solid-State nmr.
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Authors
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V.Chevelkov,
K.Faelber,
A.Diehl,
U.Heinemann,
H.Oschkinat,
B.Reif.
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Ref.
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J Biomol Nmr, 2005,
31,
295-310.
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PubMed id
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Abstract
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Water molecules are a major determinant of protein stability and are important
for understanding protein-protein interactions. We present two experiments which
allow to measure first the effective T(2) decay rate of individual amide proton,
and second the magnetization build-up rates for a selective transfer from H(2)O
to H(N) using spin diffusion as a mixing element. The experiments are
demonstrated for a uniformly (2)H, (15)N labeled sample of a microcrystalline
SH3 domain in which exchangeable deuterons were back-substituted with protons.
In order to evaluate the NMR experimental data, as X-ray structure of the
protein was determined using the same crystallization protocol as for the
solid-state NMR sample. The NMR experimental data are correlated with the
dipolar couplings calculated from H(2)O-H(N) distances which were extracted from
the X-ray structure of the protein. We find that the H(N) T(2) decay rates and
H(2)O-H(N) build-up rates are sensitive to distance and dynamics of the detected
water molecules with respect to the protein. We show that qualitative
information about localization and dynamics of internal water molecules can be
obtained in the solid-state by interpretation of the spin dynamics of a reporter
amide proton.
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