Touring the landscapes: partially folded proteins examined by hydrogen exchange
- 1 July 1997
- Vol. 5 (7) , 859-863
- https://doi.org/10.1016/s0969-2126(97)00240-2
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditionsNature Structural & Molecular Biology, 1997
- Mechanisms and uses of hydrogen exchangeCurrent Opinion in Structural Biology, 1996
- Structure of the Acid State of Escherichia coli Ribonuclease HIBiochemistry, 1996
- Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR StudyBiochemistry, 1995
- Protein Folding Intermediates: Native-State Hydrogen ExchangeScience, 1995
- Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded stateProtein Science, 1994
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins-Structure Function and Bioinformatics, 1989
- Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMRNature, 1988
- NMR evidence for an early framework intermediate on the folding pathway of ribonuclease ANature, 1988
- Hydrogen exchange and structural dynamics of proteins and nucleic acidsQuarterly Reviews of Biophysics, 1983