Collective Excitations in Protein as a Measure of Balance Between its Softness and Rigidity
[2];
[1]
- Wayne State Univ., Detroit, MI (United States). Dept. of Physics and Astronomy
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Computational Science and Engineering Division
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Chemical and Engineering Materials Division
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Biology and Soft Matter Division
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source
Here, we elucidate the protein activity from the perspective of protein softness and flexibility by studying the collective phonon-like excitations in a globular protein, human serum albumin (HSA), and taking advantage of the state-of-the-art inelastic X-ray scattering (IXS) technique. Such excitations demonstrate that the protein becomes softer upon thermal denaturation due to disruption of weak noncovalent bonds. On the other hand, no significant change in the local excitations is detected in ligand- (drugs) bound HSA compared to the ligand-free HSA. These results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER); National Science Foundation (NSF)
- Grant/Contract Number:
- AC05-00OR22725; AC02-06CH11357; 1616008
- OSTI ID:
- 1407729
- Alternate ID(s):
- OSTI ID: 1413758
- Journal Information:
- Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry, Vol. 121, Issue 5; ISSN 1520-6106
- Publisher:
- American Chemical SocietyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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