Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.

ABSTRACT: Circular Dichroism (CD) spectroscopy is a powerful method for investigating conformational changes in proteins and therefore has numerous applications in structural and molecular biology. Here a computational investigation of the CD spectrum of the Human Carbonic Anhydrase II (HCAII), with main focus on the near-UV CD spectra of the wild-type enzyme and it seven tryptophan mutant forms, is presented and compared to experimental studies. Multilevel computational methods (Molecular Dynamics, Semiempirical Quantum Mechanics, Time-Dependent Density Functional Theory) were applied in order to gain insight into the mechanisms of interaction between the aromatic chromophores within the protein environment and understand how the conformational flexibility of the protein influences these mechanisms

SUBMITTER: Karabencheva-Christova TG 

PROVIDER: S-EPMC3582176 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature