Transition dipole coupling modeling of optical activity enhancements in macromolecular protein systems

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00489322" target="_blank" >RIV/61388963:_____/18:00489322 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22340/18:43916390

Výsledek na webu

<a href="http://dx.doi.org/10.1002/chir.22778" target="_blank" >http://dx.doi.org/10.1002/chir.22778</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/chir.22778" target="_blank" >10.1002/chir.22778</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Transition dipole coupling modeling of optical activity enhancements in macromolecular protein systems

Popis výsledku v původním jazyce

Optical activity of regular molecular assemblies, such as protein fibrils or nucleic acid condensates, is often significantly stronger than for isolated molecules. Previous modeling suggested that this may be caused by the ordered quasi-periodic structure and a long-order synchronization of chromophore excitations. In the present study, we briefly review this phenomenon and investigate some aspects on simple models related to protein vibrational optical activity. The transition dipole coupling (TDC) model is used to generate vibrational circular dichroism (VCD) and Raman optical activity (ROA) spectra. While a linear arrangement of chromophores produced relatively simple couplet intensity patterns, a richer band structure was predicted for planar geometries. A stacking of beta-sheet planes has been identified as another powerful source of the enhancement. The results do not completely reproduce experimental observations but are consistent with them and confirm that chiroptical methods may be extremely useful to study aggregation of chiral molecules.

Název v anglickém jazyce

Transition dipole coupling modeling of optical activity enhancements in macromolecular protein systems

Popis výsledku anglicky

Optical activity of regular molecular assemblies, such as protein fibrils or nucleic acid condensates, is often significantly stronger than for isolated molecules. Previous modeling suggested that this may be caused by the ordered quasi-periodic structure and a long-order synchronization of chromophore excitations. In the present study, we briefly review this phenomenon and investigate some aspects on simple models related to protein vibrational optical activity. The transition dipole coupling (TDC) model is used to generate vibrational circular dichroism (VCD) and Raman optical activity (ROA) spectra. While a linear arrangement of chromophores produced relatively simple couplet intensity patterns, a richer band structure was predicted for planar geometries. A stacking of beta-sheet planes has been identified as another powerful source of the enhancement. The results do not completely reproduce experimental observations but are consistent with them and confirm that chiroptical methods may be extremely useful to study aggregation of chiral molecules.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Chirality

ISSN

0899-0042

e-ISSN

—

Svazek periodika

30

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

55-64

Kód UT WoS článku

000419238300005

EID výsledku v databázi Scopus

2-s2.0-85033231749