Collective Excitations in Protein as a Measure of Balance Between its Softness and Rigidity [electronic resource]

• Ngôn ngữ: eng
• Ký hiệu phân loại: 572.8 Biochemical genetics
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2017
• Mô tả vật lý: Size: p. 923-930 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 261988
• Chủ đề: 1. 59 basic biological sciences; 2. 60 applied life sciences; 3. Ixs; 4. Phonons; 5. Proteins

Tóm tắt

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.