Modeling of Multicolor Single-Molecule Förster Resonance Energy-Transfer Experiments on Protein Folding

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Modeling of Multicolor Single-Molecule Förster Resonance Energy-Transfer Experiments on Protein Folding. / Andryushchenko, Vladimir A.; Chekmarev, Sergei F.

в: Journal of Physical Chemistry B, Том 122, № 47, 29.11.2018, стр. 10678-10685.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

BibTeX

@article{71eb7a36b5e84201861a691d8a54cbce,

title = "Modeling of Multicolor Single-Molecule F{\"o}rster Resonance Energy-Transfer Experiments on Protein Folding",

abstract = "Using a coarse-grained, Cα-model of BBL protein, a multicolor single-molecule F{\"o}rster resonance energy transfer (FRET) experiment is modeled. Three fluorophores are introduced, which, for simplicity, are associated with Cα beads. Two fluorophores are placed at the ends of protein chain and the third one at the middle of the chain. The free-energy surfaces (FESs) depending on the interfluorophore distances and on the FRET efficiencies corresponding to these distances have been constructed and compared with the FESs depending on the conventional collective variables, such as the fraction of native contacts and radius of gyration. It has been found that multicolor experiments can successfully resolve all essential BBL states that are revealed by the conventional FESs. The resolution of these states with the FRET-efficiency histogram is found to be successful if the energy transfer is measured between the fluorophores at the BBL ends. We also show that, although the present model construct of BBL is very simple, it captures some characteristic features of the single-molecule FRET experiments, such as the pattern of the FRET-efficiency histograms and their evolution with the denaturant concentration.",

keywords = "DIMENSIONAL REACTION COORDINATE, FRET SPECTROSCOPY, DYNAMICS, SIMULATION, MECHANISMS, STATES, FORCE, RATES",

author = "Andryushchenko, {Vladimir A.} and Chekmarev, {Sergei F.}",

note = "Publisher Copyright: Copyright {\textcopyright} 2018 American Chemical Society.",

year = "2018",

month = nov,

day = "29",

doi = "10.1021/acs.jpcb.8b07737",

language = "English",

volume = "122",

pages = "10678--10685",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

publisher = "American Chemical Society",

number = "47",

}

RIS

TY - JOUR

T1 - Modeling of Multicolor Single-Molecule Förster Resonance Energy-Transfer Experiments on Protein Folding

AU - Andryushchenko, Vladimir A.

AU - Chekmarev, Sergei F.

PY - 2018/11/29

Y1 - 2018/11/29

N2 - Using a coarse-grained, Cα-model of BBL protein, a multicolor single-molecule Förster resonance energy transfer (FRET) experiment is modeled. Three fluorophores are introduced, which, for simplicity, are associated with Cα beads. Two fluorophores are placed at the ends of protein chain and the third one at the middle of the chain. The free-energy surfaces (FESs) depending on the interfluorophore distances and on the FRET efficiencies corresponding to these distances have been constructed and compared with the FESs depending on the conventional collective variables, such as the fraction of native contacts and radius of gyration. It has been found that multicolor experiments can successfully resolve all essential BBL states that are revealed by the conventional FESs. The resolution of these states with the FRET-efficiency histogram is found to be successful if the energy transfer is measured between the fluorophores at the BBL ends. We also show that, although the present model construct of BBL is very simple, it captures some characteristic features of the single-molecule FRET experiments, such as the pattern of the FRET-efficiency histograms and their evolution with the denaturant concentration.

AB - Using a coarse-grained, Cα-model of BBL protein, a multicolor single-molecule Förster resonance energy transfer (FRET) experiment is modeled. Three fluorophores are introduced, which, for simplicity, are associated with Cα beads. Two fluorophores are placed at the ends of protein chain and the third one at the middle of the chain. The free-energy surfaces (FESs) depending on the interfluorophore distances and on the FRET efficiencies corresponding to these distances have been constructed and compared with the FESs depending on the conventional collective variables, such as the fraction of native contacts and radius of gyration. It has been found that multicolor experiments can successfully resolve all essential BBL states that are revealed by the conventional FESs. The resolution of these states with the FRET-efficiency histogram is found to be successful if the energy transfer is measured between the fluorophores at the BBL ends. We also show that, although the present model construct of BBL is very simple, it captures some characteristic features of the single-molecule FRET experiments, such as the pattern of the FRET-efficiency histograms and their evolution with the denaturant concentration.

KW - DIMENSIONAL REACTION COORDINATE

KW - FRET SPECTROSCOPY

KW - DYNAMICS

KW - SIMULATION

KW - MECHANISMS

KW - STATES

KW - FORCE

KW - RATES

UR - http://www.scopus.com/inward/record.url?scp=85057561039&partnerID=8YFLogxK

U2 - 10.1021/acs.jpcb.8b07737

DO - 10.1021/acs.jpcb.8b07737

M3 - Article

C2 - 30383961

AN - SCOPUS:85057561039

VL - 122

SP - 10678

EP - 10685

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

SN - 1520-6106

IS - 47

ER -

ID: 17670287