How Soft Is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering
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- 2 June 2000
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 288 (5471) , 1604-1607
- https://doi.org/10.1126/science.288.5471.1604
Abstract
An effective environmental force constant is introduced to quantify the molecular resilience (or its opposite, “softness”) of a protein structure and relate it to biological function and activity. Specific resilience-function relations were found in neutron-scattering experiments on purple membranes containing bacteriorhodopsin, the light-activated proton pump of halobacteria; the connection between resilience and stability is illustrated by a study of myoglobin in different environments. Important advantages of the neutron method are that it can characterize the dynamics of any type of biological sample—which need not be crystalline or monodisperse—and that it enables researchers to focus on the dynamics of specific parts of a complex structure with deuterium labeling.Keywords
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