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Kwon, Oh Hoon
Ultrafast Laser Spectroscopy and Nano-microscopy (ULSaN Lab)
Research Interests
  • Femtochemistry/biology, 4D electron microscopy, structural dynamics, materials phenomena

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Solvation in protein (un)folding of melittin tetramer-monomer transition

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Title
Solvation in protein (un)folding of melittin tetramer-monomer transition
Author
Othon, Christina M.Kwon, Oh HoonLin, Milo M.Zewail, Ahmed H.
Issue Date
2009-08
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.106, no.31, pp.12593 - 12598
Abstract
Protein structural integrity and flexibility are intimately tied to solvation. Here, we examine the effect that changes in bulk and local solvent properties have on protein structure and stability. We observe the change in solvation of an unfolding of the protein model, melittin, in the presence of a denaturant, trifluoroethanol. The peptide system displays a well defined transition in that the tetramer unfolds without disrupting the secondary or tertiary structure. In the absence of local structural perturbation, we are able to reveal exclusively the role of solvation dynamics in protein structure stabilization and the (un)folding pathway. A sudden retardation in solvent dynamics, which is coupled to the change in protein structure, is observed at a critical trifluoroethanol concentration. The large amplitude conformational changes are regulated by the local solvent hydrophobicity and bulk solvent viscosity.
URI
https://scholarworks.unist.ac.kr/handle/201301/8737
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=69149100640
DOI
10.1073/pnas.0905967106
ISSN
0027-8424
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CHM_Journal Papers
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