Observation of Ultrafast Vibrational Energy Transfer in Fibrinogen and Fibrin Fibers

We study the secondary structure of the blood protein fibrinogen using two-dimensional infrared spectroscopy. With this technique, we identify the amide I′ vibrational modes of the antiparallel β-sheets and turns of fibrinogen. We observe ultrafast energy flow among these amide I′ vibrational modes...

Full description

Saved in:
Bibliographic Details
Published inThe journal of physical chemistry. B Vol. 122; no. 22; pp. 5870 - 5876
Main Authors Dutta, Biplab, Vos, Bart E, Rezus, Yves L. A, Koenderink, Gijsje H, Bakker, Huib J
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 07.06.2018
Subjects
energy flow
Energy Transfer
fibrin
Fibrin - chemistry
Fibrin - metabolism
fibrinogen
Fibrinogen - chemistry
Fibrinogen - metabolism
Humans
infrared spectroscopy
Kinetics
physical chemistry
Polymerization
Protein Conformation, beta-Strand
Spectrophotometry, Infrared
Online AccessGet full text

Cover

More Information
Summary:We study the secondary structure of the blood protein fibrinogen using two-dimensional infrared spectroscopy. With this technique, we identify the amide I′ vibrational modes of the antiparallel β-sheets and turns of fibrinogen. We observe ultrafast energy flow among these amide I′ vibrational modes with a time constant of ∼7 ps. This energy transfer time constant does not change significantly upon fibrin fiber formation, indicating that the secondary structure of the fibrinogen monomers remains largely unchanged in the polymerization process.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1520-6106
1520-5207
1520-5207
DOI:10.1021/acs.jpcb.8b03490