期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 118, 期 26, 页码 7317-7326出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp503788r
关键词
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资金
- Department of Energy support through the EPSCoR program [DE-FG02-08ER46528]
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. DOE
- UT-Battelle, LLC
- U.S. Department of Energy [DEAC05-00OR22725]
The emergence of intrinsically disordered proteins (IDPs) as a recognized structural class has forced the community to confront a new paradigm of structure, dynamics, and mechanical properties for proteins. We present novel data on the similarities and differences in the dynamics and nanomechanical properties of IDPs and other biomacromolecules on the picosecond time scale. An IDP, beta-casein (CAS), has been studied in a calcium bound and unbound state using neutron and light scattering techniques. We show that CAS partially folds and stiffens upon calcium binding, but in the unfolded state, it is softer than folded proteins such as green fluorescence protein (GFP). We also see that some localized diffusive motions in CAS have a larger amplitude than in GFP at this time scale but are still smaller than those observed in tRNA. In spite of these differences, CAS dynamics are consistent with the classes of motions seen in folded protein on this time scale.
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