Compaction during Protein Folding Studied by Real-Time NMR Diffusion Experiments
- 31 May 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (24) , 5887-5888
- https://doi.org/10.1021/ja994514d
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbuminJournal of Molecular Biology, 1999
- Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scatteringJournal of Molecular Biology, 1999
- Compactness of the kinetic molten globule of bovineα‐lactalbumin: A dynamic light scattering studyProtein Science, 1998
- Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopyJournal of Molecular Biology, 1998
- Structural characterization of the molten globule of α‐lactalbumin by solution X‐ray scatteringProtein Science, 1997
- Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray ScatteringJournal of Molecular Biology, 1996
- The Radius of Gyration of an Apomyoglobin Folding IntermediateScience, 1995
- Following protein folding in real time using NMR spectroscopyNature Structural & Molecular Biology, 1995
- Structural Characterization of the Molten Globule and Native States of Apomyoglobin by Solution X-ray ScatteringJournal of Molecular Biology, 1995
- Mutations can cause large changes in the conformation of a denatured proteinBiochemistry, 1993