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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5995459PMC
http://dx.doi.org/10.1021/acs.jpcb.8b03490DOI Listing

Publication Analysis

Top Keywords

energy transfer
8
secondary structure
8
amide vibrational
8
vibrational modes
8
time constant
8
observation ultrafast
4
ultrafast vibrational
4
vibrational energy
4
fibrinogen
4
transfer fibrinogen
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!