Conformational Effects on the Circular Dichroism of Human Carbonic Anhydrase II: A Multilevel Computational Study
2013 (English)In: PLoS ONE, ISSN 1932-6203, Vol. 8, no 2Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
Public Library of Science , 2013. Vol. 8, no 2
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-92709DOI: 10.1371/journal.pone.0056874ISI: 000316849500038OAI: oai:DiVA.org:liu-92709DiVA: diva2:621642
Funding Agencies|UK National Service for Computational Chemistry Software||UK National Supercomputer Service Hector||Marie Curie Fellowships (FP7 of EU)||2013-05-162013-05-162013-05-22