Department of Chemistry

Jane Clarke Publications (2008)

Studying the folding of multidomain proteins.
Batey S, Nickson AA, Clarke J
2008, 4, 365-377. DOI: 10.2976/1.2991513

Manipulating the stability of fibronectin type III domains by protein engineering
Ng SP, Billings KS, Randles LG, Clarke J
NANOTECHNOLOGY 2008, 0, -. DOI: 10.1088/0957-4484/19/38/384023

Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder.
Nickson AA, Stoll KE, Clarke J
Entropy, Escherichia coli, Escherichia coli Proteins, Hydrogen-Ion Concentration, Kinetics, Models, Molecular, Mutation, Protein Denaturation, Protein Engineering, Protein Folding, Protein Renaturation, Protein Structure, Tertiary, Temperature, Thermodynamics 2008, 6, 557-569. DOI: 10.1016/j.jmb.2008.05.020

The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.
Batey S, Clarke J
Animals, Chickens, Humans, Kinetics, Mutation, Protein Folding, Protein Structure, Tertiary, Spectrin 2008, 8, 297-301. DOI: 10.1016/j.jmb.2008.02.032

Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.
Geierhaas CD, Salvatella X, Clarke J, Vendruscolo M
Kinetics, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Folding, Proteins, Thermodynamics 2008, 4, 215-222. DOI: 10.1093/protein/gzm092

Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.
Randles LG, Batey S, Steward A, Clarke J
Animals, Chickens, Humans, Kinetics, Muscle Proteins, Protein Denaturation, Protein Folding, Protein Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Spectrin, Thermodynamics 2008, 5, 622-628. DOI: 10.1529/biophysj.107.119123

Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain.
Billings KS, Best RB, Rutherford TJ, Clarke J
Amino Acid Sequence, Cell Adhesion, Fibronectins, Genetic Variation, Guanidines, Humans, Hydrogen, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Isothiocyanates, Kinetics, Models, Chemical, Models, Molecular, Molecular Sequence Data, Mutant Chimeric Proteins, Mutation, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Surface Properties, Tenascin, Thermodynamics, Urea 2008, 8, 560-571. DOI: 10.1016/j.jmb.2007.10.056

Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain.
Lappalainen I, Hurley MG, Clarke J
Amino Acid Sequence, Amino Acids, Aromatic, Bacillus, Chitinase, Conserved Sequence, Fibronectins, Humans, Hydrogen Bonding, Immunoglobulins, Kinetics, Models, Chemical, Models, Molecular, Molecular Sequence Data, Mutation, Protein Denaturation, Protein Folding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Tenascin, Thermodynamics 2008, 14, 547-559. DOI: 10.1016/j.jmb.2007.09.088

Single-molecule studies of protein folding.
Borgia A, Williams PM, Clarke J
Animals, Biochemistry, Dose-Response Relationship, Drug, Fluorescence Resonance Energy Transfer, Humans, Kinetics, Microscopy, Atomic Force, Nanotechnology, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Thermodynamics, Time Factors 2008, 75, 101-125. DOI: 10.1146/annurev.biochem.77.060706.093102

An effective strategy for the design of proteins with enhanced mechanical stability.
Borgia A, Steward A, Clarke J
Amino Acid Sequence, Fibronectins, Humans, Mechanics, Microscopy, Atomic Force, Molecular Sequence Data, Protein Engineering, Protein Folding, Protein Structure, Tertiary 2008, 13, 6900-6903. DOI: 10.1002/anie.200801761