Collective Excitations in Protein as a Measure of Balance between its Softness and Rigidity

Utsab R. Shrestha; Debsindhu Bhowmik; Kurt W. Van Delinder; Eugene Mamontov; Hugh O'Neill; Qiu Zhang; Ahmet Alatas; Xiang-Qiang Chu

doi:10.1021/acs.jpcb.6b10245

Collective Excitations in Protein as a Measure of Balance between its Softness and Rigidity

Utsab R. Shrestha
, Debsindhu Bhowmik
, Kurt W. Van Delinder
, Eugene Mamontov
, Hugh O'Neill
, Qiu Zhang
, Ahmet Alatas
, Xiang-Qiang Chu^*

^*Corresponding author for this work

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

3 Citations (Scopus)

Abstract

In this article, 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. Our results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity.

Original language	English
Pages (from-to)	923-930
Journal	The Journal of Physical Chemistry B
Volume	121
Issue number	5
DOIs	https://doi.org/10.1021/acs.jpcb.6b10245
Publication status	Published - 9 Feb 2017
Externally published	Yes

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Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

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title = "Collective Excitations in Protein as a Measure of Balance between its Softness and Rigidity",

abstract = "In this article, 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. Our results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity.",

author = "Shrestha, \{Utsab R.\} and Debsindhu Bhowmik and \{Van Delinder\}, \{Kurt W.\} and Eugene Mamontov and Hugh O'Neill and Qiu Zhang and Ahmet Alatas and Xiang-Qiang Chu",

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TY - JOUR

T1 - Collective Excitations in Protein as a Measure of Balance between its Softness and Rigidity

AU - Shrestha, Utsab R.

AU - Bhowmik, Debsindhu

AU - Van Delinder, Kurt W.

AU - Mamontov, Eugene

AU - O'Neill, Hugh

AU - Zhang, Qiu

AU - Alatas, Ahmet

AU - Chu, Xiang-Qiang

N1 - Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].

PY - 2017/2/9

Y1 - 2017/2/9

N2 - In this article, 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. Our results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity.

AB - In this article, 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. Our results clearly suggest that the protein conformational flexibility and rigidity are balanced by the native protein structure for biological activity.

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UR - https://www.scopus.com/record/pubmetrics.uri?eid=2-s2.0-85026835773&origin=recordpage

U2 - 10.1021/acs.jpcb.6b10245

DO - 10.1021/acs.jpcb.6b10245

M3 - RGC 21 - Publication in refereed journal

C2 - 28080064

SN - 1520-6106

VL - 121

SP - 923

EP - 930

JO - The Journal of Physical Chemistry B

JF - The Journal of Physical Chemistry B

IS - 5

ER -

Collective Excitations in Protein as a Measure of Balance between its Softness and Rigidity

Abstract

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