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WW: An isolated three-stranded antiparallel β-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state

Academic Article
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Overview

related to degree

  • Petrassi, Mike, Ph.D. in Chemistry, Scripps Research 1997 - 2001

authors

  • Koepf, E. K.
  • Petrassi, Mike
  • Sudol, M.
  • Kelly, Jeffery

publication date

  • 1999

journal

  • Protein Science  Journal

abstract

  • The objective of this study was to evaluate the suitability of the WW domain as a desirable model system to understand the folding and stability of an isolated three-stranded antiparallel beta-sheet structure. The WW domain was subjected to thermal and chaotropic denaturation/reconstitution utilizing a variety of biophysical methods. This three-stranded sheet folds reversibly and cooperatively utilizing both urea and GdnHCl as denaturants; however, the denatured state retains structure in the form of a hydrophobic cluster involving at least one aromatic side chain. In contrast to chaotropic denaturation, thermal denaturation appears to be more complete and may be a two state process. The suitability of the WW domain for future studies aimed at understanding the kinetics and thermodynamics of antiparallel beta-sheet folding clearly emerges from this initial study. The most exciting and significant result in this manuscript is the finding that the chaotropic denatured state of WW has a hydrophobic cluster as discerned by near-UV CD evidence. The role that the denatured state plays in the folding and stability of a three-stranded beta-sheets, and its capacity for preventing aggregation may be particularly important and is the subject of ongoing studies.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Biochemical Phenomena
  • Carrier Proteins
  • Circular Dichroism
  • Dose-Response Relationship, Drug
  • Guanidine
  • Humans
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Statistical
  • Phosphoproteins
  • Protein Binding
  • Protein Denaturation
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Spectrometry, Fluorescence
  • Temperature
  • Thermodynamics
  • Urea
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Research

keywords

  • WW
  • beta-sheet folding
  • hydrophobic cluster
  • reversible folding
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Identity

PubMed Central ID

  • PMC2144315

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1110/ps.8.4.841

PubMed ID

  • 10211830
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Additional Document Info

start page

  • 841

end page

  • 853

volume

  • 8

issue

  • 4

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