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Biochemistry|May 3, 1994
Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probesL S Itzhaki, P A Evans, C M Dobson, et al.European Journal of Biochemistry|December 1, 1978
Complete assignment of aromatic 1H nuclear magnetic resonances of the tyrosine residues of hen lysozymeC M Dobson, S J Ferguson, F M Poulsen, et al.Trends in Biochemical Sciences|June 29, 2000
Understanding protein folding via free-energy surfaces from theory and experimentA R Dinner, A Sali, L J Smith, et al.The Journal of Biological Chemistry|August 2, 2001
Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphataseN Taddei, C Capanni, F Chiti, et al.Protein Science : a Publication of the Protein Society|December 6, 2000
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopyM Bouchard, J Zurdo, E J Nettleton, et al.Biochemistry|August 29, 1995
Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changesL J Smith, A E Mark, C M Dobson, et al.Biochemistry|June 1, 1993
Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange studyC L Chyan, C Wormald, C M Dobson, et al.Biochemistry|November 9, 1993
Partially folded states of equine lysozyme. Structural characterization and significance for protein foldingH Van Dael, P Haezebrouck, L Morozova, et al.Biochemistry|February 23, 1993
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR studyA T Alexandrescu, P A Evans, M Pitkeathly, et al.Journal of Molecular Biology|August 23, 1996
Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozymeK A Bolin, M Pitkeathly, A Miranker, et al.Pageof 40