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-Reference-Cited by-同舟云学术

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

Published:2008-12-31 Issue:4 Volume:8 Page:841-853
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Koepf Edward K.,Petrassi H. Michael,Sudol Marius,Kelly Jeffery W.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference63 articles.

1. α-Helix formation by peptides of defined sequence;Baldwin;Biophys Chem,1995

2. An efficient method for anchoring Fmoc-amino acids to hydroxyl-functionalised solid supports;Blankenmeyer-Menge;Tetrahedron,1990

3. The WW domin: A signaling site in dystrophin?;Bork;TIBS,1994

4. Chemical synthesis of a circular protein domain: Evidence for folding-assisted cyclization;Camarero;Angew Chem Int Ed,1998

5. Characterization of the WW domain of human Yes-associated protein and its polyproline-containing ligands;Chen;J Biol Chem,1997

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