P. Evans

发表

Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.

B. Kuhlman, D. Raleigh, D. Luisi, 1999, Journal of Molecular Biology.

Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9.

B. Kuhlman, D. Raleigh, D. Luisi, 1998, Journal of molecular biology.

Solvent isotope effects on the refolding kinetics of hen egg‐white lysozyme

L. Itzhaki, P. A. Evans, P. Evans, 1996, Protein science : a publication of the Protein Society.

Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes.

C. Dobson, S. Radford, L. Itzhaki, 1994, Biochemistry.

The folding of hen lysozyme involves partially structured intermediates and multiple pathways

C. Dobson, S. Radford, P. A. Evans, 1992, Nature.

Hydrophobic clustering in nonnative states of a protein: Interpretation of chemical shifts in NMR spectra of denatured states of lysozyme

C. Dobson, D. Woolfson, P. A. Evans, 1991, Proteins.

Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding

Dudley H. Williams, A. Raine, Rosa Zerella, 2000, Protein science : a publication of the Protein Society.

Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis

C. Dobson, P. A. Evans, G. Hatfull, 1987, Nature.

Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy

C. Dobson, P. A. Evans, R. Fox, 1986, Nature.

Understanding how proteins fold: the lysozyme story so far.

C M Dobson, C. Dobson, S. Radford, 1994, Trends in biochemical sciences.

A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease.

C. Dobson, P. A. Evans, R. Kautz, 1989, Biochemistry.

A peptide model for proline isomerism in the unfolded state of staphylococcal nuclease.

C. Dobson, D. Raleigh, M. Pitkeathly, 1992, Journal of molecular biology.

Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin.

D N Woolfson, Dudley H. Williams, D. Woolfson, 1993, Journal of molecular biology.

Hydrogen exchange in native and denatured states of hen egg‐white lysozyme

C. Dobson, S. Radford, M. Buck, 1992, Proteins.

Probing the structure of folding intermediates

S. Radford, P. A. Evans, P. Evans, 1994 .

Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study.

C M Dobson, C. Dobson, J. Baum, 1993, Biochemistry.

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin.

C M Dobson, C. Dobson, J. Baum, 1989, Biochemistry.

Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.

C M Dobson, C. Dobson, J. Baum, 1993, Biochemistry.

Protein folding kinetics from magnetization transfer nuclear magnetic resonance

C. Dobson, P. A. Evans, P. Evans, 1984 .

Protein folding in the absence of the solvent ordering contribution to the hydrophobic interaction.

D. Woolfson, D. Williams, A. Cooper, 1993, Journal of molecular biology.

Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates

P. A. Evans, Markus Engelhard, P. Evans, 1995, Protein science : a publication of the Protein Society.

Autonomous folding of a peptide corresponding to the N‐terminal β‐hairpin from ubiquitin

John M. C. Ionides, Dudley H. Williams, J. Ionides, 1999, Protein science : a publication of the Protein Society.