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Dynamics of proteins in solution

QUARTERLY REVIEWS OF BIOPHYSICS(2019)

Cited 87|Views31
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Abstract
The dynamics of proteins in solution includes a variety of processes, such as backbone and side-chain fluctuations, interdomain motions, as well as global rotational and translational (i.e. center of mass) diffusion. Since protein dynamics is related to protein function and essential transport processes, a detailed mechanistic understanding and monitoring of protein dynamics in solution is highly desirable. The hierarchical character of protein dynamics requires experimental tools addressing a broad range of time- and length scales. We discuss how different techniques contribute to a comprehensive picture of protein dynamics, and focus in particular on results from neutron spectroscopy. We outline the underlying principles and review available instrumentation as well as related analysis frameworks.
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Key words
Quasielastic neutron spectroscopy,protein diffusion,protein backbone,protein side chains,molecular relaxations,colloid physics
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