Premium
Triplet–triplet energy transfer studies on conformational dynamics in peptides and a protein
Author(s) -
Reiner Andreas
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1353
Subject(s) - chemistry , microsecond , nanosecond , molecular dynamics , folding (dsp implementation) , protein folding , kinetics , villin , förster resonance energy transfer , chemical physics , van der waals force , helix (gastropod) , protein dynamics , molecule , computational chemistry , fluorescence , physics , actin , ecology , laser , biochemistry , electrical engineering , organic chemistry , quantum mechanics , astronomy , snail , optics , biology , engineering
Peptides and proteins are highly dynamic systems, which can adopt more or less stable conformations. The dynamics of these molecules, particularly those on the nanosecond to tens of microsecond time scale, are difficult to assess with conventional techniques. This review summarizes experiments using TTET, a technique that reports on van der Waals contact formation between a triplet donor and acceptor group, and which is sensitive in this time range. TTET allows to directly measure the chain dynamics of unstructured model peptides, i.e. large‐amplitude fluctuations on the nanosecond time scale. Furthermore, contact formation can be used as irreversible probing reaction to study the kinetics of conformational equilibria. This approach enabled us to measure local α‐helix folding and unfolding in helical peptides, which gave new insight into the equilibrium dynamics of this fundamental secondary structure element. TTET has also been applied to study the dynamics both in the native and unfolded state of a protein, the villin headpiece subdomain. The contact formation kinetics between different positions revealed an unlocking and local unfolding reaction in the native state of this model protein, and gave information about the chain dynamics in the unfolded state ensemble. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.