Abstract
Protein engineering studies show that conformations in the folding transition state ensemble can be structurally polarized. In two SH3 β-sheet domains, the formation of hydrophobic contacts goes hand in hand with the formation of the solvated distal loop β-turn, while large parts of the molecule remain unstructured in the ensemble.
Original language | English (US) |
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Pages (from-to) | 662-665 |
Number of pages | 4 |
Journal | Nature Structural and Molecular Biology |
Volume | 5 |
Issue number | 8 |
DOIs | |
State | Published - Aug 1998 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology