Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor
Open Access
- 1 September 1997
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 6 (9) , 1985-1992
- https://doi.org/10.1002/pro.5560060919
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Local fluctuations and global unfolding of partially folded BPTI detected by NMRBiophysical Chemistry, 1997
- From Levinthal to pathways to funnelsNature Structural & Molecular Biology, 1997
- A Lysozyme Folding Intermediate Revealed by Solution X-ray ScatteringJournal of Molecular Biology, 1996
- Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor (BPTI) analoguesTechniques in Protein Chemistry, 1996
- Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslinkFolding and Design, 1996
- Dynamic Structure of a Highly Ordered .beta.-Sheet Molten Globule: Multiple Conformations with a Stable CoreBiochemistry, 1995
- Association of Biomolecular Systems via Pulsed Field Gradient NMR Self-Diffusion MeasurementsJournal of the American Chemical Society, 1995
- Principles of protein folding — A perspective from simple exact modelsProtein Science, 1995
- Estimation of intramolecular distance distributions in bovine pancreatic trypsin inhibitor by site-specific labeling and nonradiative excitation energy-transfer measurementsBiochemistry, 1987
- Theory for the folding and stability of globular proteinsBiochemistry, 1985