Pages that link to "Q71715115"
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The following pages link to Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable core (Q71715115):
Displaying 14 items.
- BetaCore, a designed water soluble four-stranded antiparallel β-sheet protein (Q27639022) (← links)
- Collapse and cooperativity in protein folding (Q30424224) (← links)
- Hydrogen exchange, core modules, and new designed proteins (Q30756166) (← links)
- Experimental approaches to protein folding based on the concept of a slow hydrogen exchange core (Q34267082) (← links)
- Early events in the disulfide-coupled folding of BPTI. (Q36281623) (← links)
- Structural analysis of non-native states of proteins by NMR methods (Q41026035) (← links)
- 27 Chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins (Q41629620) (← links)
- Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor (Q41812667) (← links)
- BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path. (Q55283783) (← links)
- Synthetic Circularized Analogues of Bovine Pancreatic Trypsin Inhibitor (Q58035753) (← links)
- Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink (Q73174186) (← links)
- Local fluctuations and global unfolding of partially folded BPTI detected by NMR (Q73289670) (← links)
- Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine β-trypsin (Q74186419) (← links)
- Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study (Q81500061) (← links)