Abstract:
:NMR relaxation experiments of isotopically labeled proteins provide a wealth of information on reorientational global and local dynamics on nanosecond and subnanosecond timescales for folded and nonfolded proteins in solution. Recent methodological advances in the interpretation of relaxation data have led to a better understanding of the overall tumbling behavior, the separability of internal and overall motions, and the presence of correlated dynamics between different nuclear sites, as well as to new insights into the relationship between reorientational dynamics and primary and tertiary protein structure. Some of the new methods are particularly useful when dealing with nonfolded protein states.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Brüschweiler Rdoi
10.1016/s0959-440x(03)00036-8subject
Has Abstractpub_date
2003-04-01 00:00:00pages
175-83issue
2eissn
0959-440Xissn
1879-033Xpii
S0959440X03000368journal_volume
13pub_type
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