Published May 2002 | Version v1
Journal article

Protein dynamics in supercooled water: The search for slow motional modes

  • 1. University at Buffalo, The State University of New York, Department of Chemistry and Structural Biology (United States)

Description

The impact of studying protein dynamics in supercooled water for identifying slow motional modes on the μs time scale is demonstrated. Backbone 15N spin relaxation parameters were measured at -13 deg. C for ubiquitin, which plays a central role for signaling proteolysis, cellular trafficking and kinase activation in eukaryotic organisms. A hitherto undetected motional mode involving Val 70 was found, which may well play an important role for ubiquitin recognition. The measurement of rotating frame 15N relaxation times as a function of the spin-lock field allowed determination of the correlation time of this motional mode, which would not have been feasible above 0 deg. C

Additional details

Identifiers

Publishing Information

Journal Title
Journal of Biomolecular NMR
Journal Volume
23
Journal Issue
1
Journal Page Range
p. 63-67
ISSN
0925-2738

INIS

Country of Publication
Netherlands
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
39109631
Subject category
S62: RADIOLOGY AND NUCLEAR MEDICINE;
Descriptors DEI
NITROGEN 15; PROTEIN STRUCTURE; PROTEINS; PROTEOLYSIS; RELAXATION
Descriptors DEC
CHEMICAL REACTIONS; DECOMPOSITION; ISOTOPES; LIGHT NUCLEI; NITROGEN ISOTOPES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; STABLE ISOTOPES

Optional Information

Copyright
Copyright (c) 2002 Kluwer Academic Publishers