Ultrafast Förster resonance energy transfer from tyrosine to tryptophan in monellin: potential intrinsic spectroscopic ruler-Reference-Cited by-同舟云学术

Ultrafast Förster resonance energy transfer from tyrosine to tryptophan in monellin: potential intrinsic spectroscopic ruler

Published:2023 Issue:10 Volume:25 Page:7239-7250
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Li Haoyang¹,Cao Simin²,Zhang Sanjun¹^ORCID,Chen Jinquan¹^ORCID,Xu Jianhua¹^ORCID,Knutson Jay R.³

Affiliation:

1. State Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China

2. Key Laboratory of 3D Micro/Nano Fabrication and Characterization of Zhejiang Province, School of Engineering, Westlake University, Hangzhou 310024, China

3. Laboratory of Advanced Microscopy & Biophotonics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA

Abstract

Schematic diagram of ultrafast energy transfer from tyrosine to tryptophan in monellin. The three tyrosines close to tryptophan transfer energy to it by FRET. The energy transfer lifetime is ∼200 ps.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D2CP05842A

Reference41 articles.

1. Dependence of Tryptophan Emission Wavelength on Conformation in Cyclic Hexapeptides

2. Dynamics of l-tryptophan in aqueous solution by simultaneous laser induced fluorescence (LIF) and photoacoustic spectroscopy (PAS)

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4. Unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy

5. Localization and Environment of Tryptophans in Soluble and Membrane-Bound States of a Pore-Forming Toxin from Staphylococcus aureus

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