Conformational effects on the Circular Dichroism of Human Carbonic Anhydrase II: a multilevel computational study

Tatyana Karabencheva-Christova, Uno Carlsson, Kia Balali-Mood, Gary Black, Christo Christov

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)
4 Downloads (Pure)

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. The analysis suggests that combining CD semi empirical calculations, crystal structures and molecular dynamics (MD) could help in achieving a better agreement between the computed and experimental protein spectra and provide some unique insight into the dynamic nature of the mechanisms of chromophore interactions.
Original languageEnglish
Pages (from-to)e56874
JournalPLoS One
Volume8
Issue number2
DOIs
Publication statusPublished - 25 Feb 2013

Fingerprint Dive into the research topics of 'Conformational effects on the Circular Dichroism of Human Carbonic Anhydrase II: a multilevel computational study'. Together they form a unique fingerprint.

Cite this