Multi-scale modeling of electronic spectra of three aromatic amino acids: importance of conformational averaging and explicit solute-solvent interactions

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10288348" target="_blank" >RIV/00216208:11310/14:10288348 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/14:00433378 RIV/00216208:11320/14:10288348

Result on the web

<a href="http://pubs.rsc.org/en/content/articlepdf/2014/cp/c4cp02668c" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2014/cp/c4cp02668c</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c4cp02668c" target="_blank" >10.1039/c4cp02668c</a>

Result language

angličtina

Original language name

Multi-scale modeling of electronic spectra of three aromatic amino acids: importance of conformational averaging and explicit solute-solvent interactions

Original language description

Electronic transitions in the ultraviolet and visible spectral range can reveal a wealth of information about biomolecular geometry and interactions, such as those involved in protein folding. However, the modeling that provides the necessary link between spectral shapes and the structure is often difficult even for seemingly simple systems. To understand as to how conformational equilibria and solute-solvent interaction influence spectral intensities, we collected absorption (UV-vis), electronic circular dichroism (ECD), and magnetic circular dichroism (MCD) spectra of phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) zwitterions in aqueous solutions, and compared them with quantum-chemical simulations. These aromatic amino acids provide a relatively strong signal in the accessible wavelength range. At the same time, they allow for a relatively accurate modeling. Energies and intensities of spectral bands were reproduced by the time-dependent density functional theory (TD DFT). The solvent was approximated by a continuum as well as clusters containing solvent molecules from the first hydration sphere. The ECD signal was found to be strongly dependent on molecular conformation, and the dependence was much weaker in UV-vis and MCD spectra. All spectral intensities, however, were significantly affected by the solvent approximation; especially for ECD and MCD the usual polarizable continuum solvent model did not yield satisfactory spectral shapes. On the other hand, averaging of the clusters obtained from molecular dynamics simulations provided an unprecedented agreement with the experiment. Proper modeling of the interactions with the environment thus makes the information about the molecular structure, as obtained from the electronic spectra, more accurate and reliable.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10403 - Physical chemistry

Project

<a href="/en/project/GAP208%2F11%2F0105" target="_blank" >GAP208/11/0105: Expanding the Optical Activity Method to the Realm of Biomolecules</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

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Volume of the periodical

16

Issue of the periodical within the volume

38

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

20639-20649

UT code for WoS article

000342072300044

EID of the result in the Scopus database

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