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  Temperature- and Photocontrolled Unfolding/Folding of a Triple-Helical Azobenzene-Stapled Collagen Peptide Monitored by Infrared Spectroscopy

Lorenz, L., Kusebauch, U., Moroder, L., & Wachtveitl, J. (2016). Temperature- and Photocontrolled Unfolding/Folding of a Triple-Helical Azobenzene-Stapled Collagen Peptide Monitored by Infrared Spectroscopy. ChemPhysChem, 17(9, Special Issue: Fast Spectroscopy of Biosystems ), 1314-1320. doi:10.1002/cphc.201501103.

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 Creators:
Lorenz, Lisa1, Author
Kusebauch, Ulrike2, Author              
Moroder, Luis2, Author              
Wachtveitl, Josef1, Author
Affiliations:
1external, ou_persistent22              
2Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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Free keywords: PICOSECOND CONFORMATIONAL TRANSITION; AMIDE-I-BAND; MOLECULAR-STRUCTURE; MODEL PEPTIDES; STABILITY; PROTEINS; POLYTRIPEPTIDES; POLYPEPTIDESChemistry; Physics; azobenzene; collagen triple helix; FTIR spectroscopy; photoisomerization; protein folding;
 Abstract: The triple-helical structure of a model collagen peptide possessing azobenzene-derived clamps integrated in all three strands as side-chain-to-side-chain crosslinks is analyzed by IR spectroscopy in comparative thermal excursion experiments with the triple helix of a typical reference collagen peptide consisting of only glycine-proline-hydroxyproline repeats. By exploiting the known stabilizing effects of aqueous alcoholic solvents on the unique collagen fold, deuterated ethylene glycol/water (1:1) is used as a solvent to investigate the effect of the light-switchable trans/cis-azobenzene clamp on the stability of the triple helix in terms of H/D exchange rates and thermal unfolding. Results of this comparative analysis clearly reveal only a minor destabilization of the triple helix by the hydrophobic azobenzene moieties compared to the reference collagen peptide as reflected by a lower midpoint of the thermal unfolding and higher rates of H/D exchange. However, it also reveals that the driving force exerted by the trans-to-cis photoisomerization of the azobenzene moieties is insufficient for unfolding of the compact triple-helical collagen fold. Only temperature-dependent untightening of this fold with heating results in a reversible photomodulated unfolding and refolding of the azo-collagen peptide into the original triple helix.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000376003400010
DOI: 10.1002/cphc.201501103
 Degree: -

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Title: ChemPhysChem
Source Genre: Journal
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Publ. Info: Weinheim, Germany : Wiley-VCH
Pages: - Volume / Issue: 17 (9, Special Issue: Fast Spectroscopy of Biosystems ) Sequence Number: - Start / End Page: 1314 - 1320 Identifier: ISSN: 1439-4235
CoNE: https://pure.mpg.de/cone/journals/resource/954925409790