Published May 2002
| Version v1
Journal article
Protein dynamics in supercooled water: The search for slow motional modes
Creators
- 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