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

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 focu...

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Autores principales:	Tatyana G Karabencheva-Christova, Uno Carlsson, Kia Balali-Mood, Gary W Black, Christo Z Christov
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/158ec676447147ad9e2e9d9d07cb82e8
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spelling	oai:doaj.org-article:158ec676447147ad9e2e9d9d07cb82e82021-11-18T07:56:00ZConformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.1932-620310.1371/journal.pone.0056874https://doaj.org/article/158ec676447147ad9e2e9d9d07cb82e82013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23526922/?tool=EBIhttps://doaj.org/toc/1932-6203Circular 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.Tatyana G Karabencheva-ChristovaUno CarlssonKia Balali-MoodGary W BlackChristo Z ChristovPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 2, p e56874 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tatyana G Karabencheva-Christova Uno Carlsson Kia Balali-Mood Gary W Black Christo Z Christov Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
description	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.
format	article
author	Tatyana G Karabencheva-Christova Uno Carlsson Kia Balali-Mood Gary W Black Christo Z Christov
author_facet	Tatyana G Karabencheva-Christova Uno Carlsson Kia Balali-Mood Gary W Black Christo Z Christov
author_sort	Tatyana G Karabencheva-Christova
title	Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
title_short	Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
title_full	Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
title_fullStr	Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
title_full_unstemmed	Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.
title_sort	conformational effects on the circular dichroism of human carbonic anhydrase ii: a multilevel computational study.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/158ec676447147ad9e2e9d9d07cb82e8
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Conformational effects on the circular dichroism of Human Carbonic Anhydrase II: a multilevel computational study.

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