LK peptide side chain dynamics at interfaces are independent of secondary structure
Author:
Affiliation:
1. Max Planck Institute for Polymer Research
2. 55128 Mainz
3. Germany
4. Department of Chemical Engineering
5. University of Washington
6. 105 Benson Hall
7. Seattle
8. USA
Abstract
Real-time observation of the ultrafast motions of leucine side chains within model peptides at the water–air interface with representative folds – α-helix, 310-helix, β-strand – show that interfacial dynamics are mostly determined by surface interactions.
Funder
Aarhus Universitets Forskningsfond
Deutsche Forschungsgemeinschaft
Directorate for Engineering
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP05897G
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5. Inelastic X-ray Scattering Studies of the Short-Time Collective Vibrational Motions in Hydrated Lysozyme Powders and Their Possible Relation to Enzymatic Function
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