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Biophysical Journal|September 22, 2001
Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulationR B Best, B Li, A Steward, et al.Journal of Molecular Biology|March 8, 2000
The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topologyS J Hamill, A Steward, J ClarkeJournal of Molecular Biology|January 12, 2001
The molecular basis for the inverse temperature transition of elastinB Li, D O Alonso, V DaggettJournal of Molecular Biology|February 13, 2001
The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like foldE Cota, A Steward, S B Fowler, et al.Proceedings of the National Academy of Sciences of the United States of America|February 12, 1998
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathwayC J Bond, K B Wong, J Clarke, et al.Protein Science : a Publication of the Protein Society|February 24, 2001
The effects of disulfide bonds on the denatured state of barnaseJ Clarke, A M Hounslow, C J Bond, et al.Current Opinion in Biotechnology|August 28, 1998
Structure-function aspects of prion proteinsV DaggettBiochemical Society Symposium|September 28, 2001
Validation of protein-unfolding transition states identified in molecular dynamics simulationsV DaggettPharmaceutical Research|August 1, 1987
Protein degradation: the role of mixed-function oxidasesV DaggettPageof 653