Loop formation in unfolded polypeptide chains on the picoseconds to microseconds time scale

Intrachain loop formation allows unfolded polypeptide chains to search for favorable interactions during protein folding. We applied triplet-triplet energy transfer between a xanthone moiety and naphthylalanine to directly measure loop formation in various unfolded polypeptide chains with loop regio...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-02, Vol.104 (7), p.2163-2168
Main Authors: Fierz, Beat, Satzger, Helmut, Root, Christopher, Gilch, Peter, Zinth, Wolfgang, Kiefhaber, Thomas
Format: Article
Language:English
Subjects:
Absorption spectra
Alanine - analogs & derivatives
Alanine - chemistry
Atomic energy levels
Biochemistry
Biological Sciences
Diffusion
Electron transfer
Energy Transfer
Exponential functions
Free energy
Kinetics
Models, Molecular
Molecules
Motion
Peptides
Peptides - chemistry
Physical Sciences
Protein Folding
Protein Structure, Secondary
Stiffness
Time constants
Time Factors
Xanthones - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Intrachain loop formation allows unfolded polypeptide chains to search for favorable interactions during protein folding. We applied triplet-triplet energy transfer between a xanthone moiety and naphthylalanine to directly measure loop formation in various unfolded polypeptide chains with loop regions consisting of polyserine, poly(glycine-serine) or polyproline. By combination of femtosecond and nanosecond laserflash experiments loop formation could be studied over many orders of magnitude in time from picoseconds to microseconds. The results reveal processes on different time scales indicating motions on different hierarchical levels of the free energy surface. A minor (
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0611087104