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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-22 2:20 |
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Conference: Bucharest University Faculty of Physics 2010 Meeting
Section: Solid State Physics and Materials Science
Title:
Toward the Physical Basis of Protein Folding: Model DMD for hydrogen bond interactions. CD and DSC experimental results on BSA
Authors:
Ana Ioanid (1), Silviu Polosan (2)
Affiliation:
(1) Faculty of Physics, University of Bucharest;
(2) National Institute Materials Physics Bucharest
E-mail
ana_ioanid@yahoo.com
Keywords:
protein folding, DMD method, CD spectroscopy, DSC analysis
Abstract:
Protein folding is a remarkable process that affects nearly every aspect of biological function. This consists in conformational changes to stabilize native structure of protein. The native conformation must be energetically stable. From a thermodynamic point of view, the free energy of a ptotein molecule is influenced by the following major contributions: (1) the hydrophobic effect, (2) the energy of hydrogen bonds, (3) the electrostatic interactions, and (4) the conformational entropy due to the restricted motion of the backbone and the side chains. We propose a DMD model for the potential energy of backbone hydrogen bond interactions. Experimental Circular Dichroism (CD) and Differential Scanning Calorimetry (DSC) studies for BSA, support the thermodynamic analysis of model.
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