Understanding how proteins fold: the lysozyme story so far
- 1 January 1994
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 19 (1), 31-37
- https://doi.org/10.1016/0968-0004(94)90171-6
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Detection of Transient Protein Folding Populations by Mass SpectrometryScience, 1993
- Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange studyBiochemistry, 1993
- Structure of Hen Lysozyme in SolutionJournal of Molecular Biology, 1993
- Structure and dynamics of the acid-denatured molten globule state of .alpha.-lactalbumin: a two-dimensional NMR studyBiochemistry, 1993
- Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozymeBiochemistry, 1992
- Crystal structure of human α-lactalbumin at 1·7 Å resolutionJournal of Molecular Biology, 1991
- Protein folding: Effect of packing density on chain conformationJournal of Molecular Biology, 1991
- Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozymeBiochemistry, 1986
- Protein folding kinetics from magnetization transfer nuclear magnetic resonanceBiochemistry, 1984
- Protein-folding dynamicsNature, 1976