Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains

This publication has 43 references indexed in Scilit:

• Multiple protein folding nuclei and the transition state ensemble in two‐state proteins
  Proteins-Structure Function and Bioinformatics, 2001
• The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.
  Nature Structural & Molecular Biology, 1999
• Experiment and theory highlight role of native state topology in SH3 folding
  Nature Structural & Molecular Biology, 1999
• Lattice models for proteins reveal multiple folding nuclei for nucleation-collapse mechanism
  Journal of Molecular Biology, 1998
• Obligatory steps in protein folding and the conformational diversity of the transition state
  Nature Structural & Molecular Biology, 1998
• Folding funnels and energy landscapes of larger proteins within the capillarity approximation
  Proceedings of the National Academy of Sciences, 1997
• Protein folding funnels: the nature of the transition state ensemble
  Folding and Design, 1996
• Conserved residues and the mechanism of protein folding
  Nature, 1996
• Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
  Biopolymers, 1995
• Characterizing transition states in protein folding: an essential step in the puzzle
  Current Opinion in Structural Biology, 1995