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

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• 作者：Utsab R. Shrestha ; Debsindhu Bhowmik ; Kurt W. Van Delinder ; Eugene Mamontov ; Hugh O’Neill ; Qiu Zhang ; Ahmet Alatas ; Xiang-Qiang Chu
• 刊名：Journal of Physical Chemistry B
• 出版年：2017
• 出版时间：February 9, 2017
• 年：2017
• 卷：121
• 期：5
• 页码：923-930
• 全文大小：562K
• ISSN：1520-5207

文摘

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.