Journal
CHEMICAL PHYSICS
Volume 422, Issue -, Pages 115-123Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chemphys.2012.11.009
Keywords
Protein folding; Helix-coil transition; Poly-glutamic acid; Temperature jump; Time-resolved IR spectroscopy
Funding
- UK Engineering and Physical Sciences Research Council (EPSRC)
- EPSRC
- Engineering and Physical Sciences Research Council [EP/G03088X/1] Funding Source: researchfish
- EPSRC [EP/G03088X/1] Funding Source: UKRI
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Poly-L-glutamic acid (PGA) is an ideal model system for investigating the transition between alpha-helical and random coil peptide conformations, since its secondary structure is highly sensitive not only to temperature, but also to pH. Laser pulse-induced temperature jumps were used to observe pH-dependent PGA helix-coil relaxation dynamics on the microsecond time scale. The relaxation was found to be non-exponential, particularly if only short helical segments are present before the temperature jump, indicating the multi-step nature of the process which involves helix nucleation and propagation. Helix-coil relaxation is slowest near the mid-point of the pH-induced helix-coil transition, in agreement with theoretical predictions. (C) 2012 Elsevier B. V. All rights reserved.
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