Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride
- 15 February 2007
- journal article
- Published by Elsevier BV in Biophysical Journal
- Vol. 92 (4), 1374-1383
- https://doi.org/10.1529/biophysj.106.091736
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Folding and binding: The conformational repertoire of proteins: folding, aggregation and structural recognitionCurrent Opinion in Structural Biology, 2006
- The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinaseBiochemical and Biophysical Research Communications, 2005
- The Yin and Yang of protein foldingThe FEBS Journal, 2005
- Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide EpoxideJournal of Molecular Biology, 2005
- pH-dependent Conformational Flexibility of the SARS-CoV Main Proteinase (Mpro) Dimer: Molecular Dynamics Simulations and Multiple X-ray Structure AnalysesJournal of Molecular Biology, 2005
- Design of Wide-Spectrum Inhibitors Targeting Coronavirus Main ProteasesPLoS Biology, 2005
- Protein folding and the organization of the protein topology universeTrends in Biochemical Sciences, 2005
- Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation ModelingBiophysical Journal, 2000
- Staphylococcal Nuclease: A Showcase of m-Value EffectsAdvances in protein chemistry, 1995
- Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutantsProtein Science, 1993