
- Structures and folding pathways of topologically knotted proteins This article has been downloaded from IOPscience. Please scroll down to see the full text article.
- Native-state dynamics of the ubiquitin family: implications for function
- The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins
- Local and long-range stability in tandemly arrayed tetratricopeptide repeats
- Ubiquitin folds through a highly polarized transition state
- The Effect of Parkinson's-Disease-Associated Mutations on the Deubiquitinating Enzyme UCH-L1
- Protein denaturation and protein:drugs interactions from intrinsic protein
- Folding Study of Venus Reveals a Strong Ion Dependence of Its Yellow Fluorescence under Mildly Acidic Conditions*S
- Experimental detection of knotted conformations in denatured proteins
- Provided for non-commercial research and educational use only. Not for reproduction, distribution or commercial use.
- The extremely slow-exchanging core and acid-denatured state of green fluorescent protein
- Exploring knotting mechanisms in protein folding Anna L. Mallam, Elizabeth R. Morris, and Sophie E. Jackson1
- Molecular Cell Short Article
- COMMUNICATION Mechanistic Studies on Hsp90 Inhibition by
- Stable Intermediate States and High Energy Barriers in the Unfolding of GFP
- The latest in Engineering and design: the 2005 collection Editorial overview
- Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data
- Native-state dynamics of the ubiquitin family: implications for function
- Independent ATPase Activity of Hsp90 Subunits Creates a Flexible Assembly Platform
- ARTICLE IN PRESS The folding pathway of ubiquitin from all-atom
- Energetic and Structural Analysis of the Role of Tryptophan 59 in FKBP12 Kate F. Fulton, Sophie E. Jackson, and Ashley M. Buckle*,
- Fast Folding of a Four-Helical Bundle Protein Neelan J. Marianayagam, Farid Khan, Louise Male, and Sophie E. Jackson*
- Stimulation of the Weak ATPase Activity of Human Hsp90 by a Client Protein
- Journal of Biological Physics 27: 99117, 2001. 2001 Kluwer Academic Publishers. Printed in the Netherlands.
- 1. Kim, P.S. & Baldwin, R.L. Annu. Rev. Biochem. 51, 459489 (1982). 2. Kim, P.S. & Baldwin, R.L. Annu. Rev. Biochem. 59, 631660 (1990).
- Mapping the Interactions Present in the Transition State for Unfolding/Folding of FKBP12
- Folding Pathway of FKBP12 and Characterisation of the Transition State
- Folding Studies on a Knotted Protein Anna L. Mallam and Sophie E. Jackson*
- Spin Relaxation Effects in Photochemically Induced Dynamic Nuclear Polarization Spectroscopy of Nuclei with Strongly
- How do small single-domain proteins fold? Sophie E Jackson
- Is an intermediate state populated on the folding pathway of ubiquitin? Heather M. Went, Claudia G. Benitez-Cardoza, Sophie E. Jackson*
- Context-Dependent Nature of Destabilizing Mutations on the Stability of FKBP12 Ewan R. G. Main, Kate F. Fulton, and Sophie E. Jackson*
- This article was published as part of the 2009 Green Fluorescent Protein issue
- The Dimerization of an a/b-Knotted Protein Is Essential for Structure and Function
- Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1)
- Evidence of an Intermediate and Parallel Pathways in Protein Unfolding from Single-Molecule Fluorescence
- This article was published as part of the 2009 Green Fluorescent Protein issue
- Probing Nature's Knots: The Folding Pathway of a Knotted Homodimeric Protein
- PERSPECTIVE www.rsc.org/obc | Organic & Biomolecular Chemistry Ubiquitin: a small protein folding paradigm
- Exploring Sequence/Folding Space: Folding Studies on Multiple Hydrophobic Core Mutants of Ubiquitin,
- A recurring theme in protein engineering: the design, stability and folding of repeat proteins
- Engineering and design Protein design: theory and practice
- Folding and stability of the ligand-binding domain of the glucocorticoid receptor
- Journal of Biomolecular NMR, 26: 281282, 2003. KLUWER/ESCOM
- Untangling the folding mechanism of the 52-knotted protein UCH-L3
- Destabilised mutants of ubiquitin gain equal stability in crowded solutions Andrew Roberts, Sophie E. Jackson
- An Independent Method for the Analysis of Protein Folding Kinetics from All-atom
- The folding and design of repeat proteins: reaching a consensus Ewan RG Mainy
- Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90
- Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90
- F NMR Studies of the Native and Denatured States of Green Fluorescent Protein
- Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes
- 2011NatureAmerica,Inc.Allrightsreserved. nature CHeMICaL BIOLOGY | AdvAnce online publicAtion | www.nature.com/naturechemicalbiology 1