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How Soft Is a Protein? A Protein Dynamics Force Constant Measured by Neutron Scattering
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.
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Cited by
THz time domain spectroscopy of biomolecular conformational modes
Markelz, A., Whitmire, S., Hillebrecht, J., & Birge, R. (2002) · Physics in Medicine and Biology · doi:10.1088/0031-9155/47/21/318 · Cited by 309
Terahertz Time-Domain Spectroscopy of Solids: A Review
Hangyo, M., Tani, M., & Nagashima, T. (2005) · International Journal of Infrared and Millimeter Waves · doi:10.1007/s10762-005-0288-1 · Cited by 258
Kim, J. Y., Oh, H., & Moon, H. R. (2019) · Advanced Materials · doi:10.1002/adma.201805293 · Cited by 174
Antibody evolution constrains conformational heterogeneity by tailoring protein dynamics
Zimmermann, J., Oakman, E. L., Thorpe, I. F., Shi, X., Abbyad, P., Brooks, C. L., Boxer, S. G., & Romesberg, F. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603282103 · Cited by 116
Unravelling the Adaptation Mechanisms to High Pressure in Proteins
Caliò, A., Dubois, C., Fontanay, S., Koza, M. M., Hoh, F., Roumestand, C., Oger, P., & Peters, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158469 · Cited by 12
Metadata
- Authors
- Zaccai, G.
- Venue
- Science
- Published
- 2000-06-02
- Volume
- 288
- Issue
- 5471
- Pages
- 1604-1607
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2155027540
- Cited by
- 733
- References
- 0
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- closed
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