Changes of Conformation in Albumin with Temperature by Molecular Dynamics Simulations.

ABSTRACT: This work presents the analysis of the conformation of albumin in the temperature range of 300 K - 312 K , i.e., in the physiological range. Using molecular dynamics simulations, we calculate values of the backbone and dihedral angles for this molecule. We analyze the global dynamic properties of albumin treated as a chain. In this range of temperature, we study parameters of the molecule and the conformational entropy derived from two angles that reflect global dynamics in the conformational space. A thorough rationalization, based on the scaling theory, for the subdiffusion Flory-De Gennes type exponent of 0 . 4 unfolds in conjunction with picking up the most appreciable fluctuations of the corresponding statistical-test parameter. These fluctuations coincide adequately with entropy fluc

SUBMITTER: Weber P 

PROVIDER: S-EPMC7516880 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature