C M Dobson

Summary

Affiliation: University of Oxford
Country: UK

Publications

  1. ncbi request reprint The fundamentals of protein folding: bringing together theory and experiment
    C M Dobson
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Curr Opin Struct Biol 9:92-101. 1999
  2. pmc The structural basis of protein folding and its links with human disease
    C M Dobson
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Philos Trans R Soc Lond B Biol Sci 356:133-45. 2001
  3. pmc Protein folding and misfolding inside and outside the cell
    C M Dobson
    Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    EMBO J 17:5251-4. 1998
  4. ncbi request reprint Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human alpha-lactalbumin
    L J Smith
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, England
    J Mol Biol 286:1567-80. 1999
  5. ncbi request reprint Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation
    E Paci
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK
    J Mol Biol 306:329-47. 2001
  6. ncbi request reprint Amyloid fibril formation by a helical cytochrome
    T A Pertinhez
    New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks, UK
    FEBS Lett 495:184-6. 2001
  7. ncbi request reprint Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy
    R Wijesinha-Bettoni
    Oxford Centre for Molecular Sciences, University of Oxford, New Chemistry Laboratory South Parks Road, Oxford, OX1 3QT, UK
    J Mol Biol 307:885-98. 2001
  8. ncbi request reprint Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds
    C Redfield
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Nat Struct Biol 6:948-52. 1999
  9. ncbi request reprint Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    J Zurdo
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, South Parks Road, Oxford, OX1 3QH, UK
    J Mol Biol 311:325-40. 2001
  10. pmc A refined solution structure of hen lysozyme determined using residual dipolar coupling data
    H Schwalbe
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, Oxford OX1 3QT, England
    Protein Sci 10:677-88. 2001

Collaborators

Detail Information

Publications23

  1. ncbi request reprint The fundamentals of protein folding: bringing together theory and experiment
    C M Dobson
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Curr Opin Struct Biol 9:92-101. 1999
    ....
  2. pmc The structural basis of protein folding and its links with human disease
    C M Dobson
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Philos Trans R Soc Lond B Biol Sci 356:133-45. 2001
    ..Understanding the nature of such protective mechanisms is a crucial step in the development of strategies to prevent and treat these debilitating diseases...
  3. pmc Protein folding and misfolding inside and outside the cell
    C M Dobson
    Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    EMBO J 17:5251-4. 1998
    ..In this report we concentrate on general concepts and themes rather than on detailing every contribution...
  4. ncbi request reprint Side-chain conformational disorder in a molten globule: molecular dynamics simulations of the A-state of human alpha-lactalbumin
    L J Smith
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, England
    J Mol Biol 286:1567-80. 1999
    ....
  5. ncbi request reprint Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation
    E Paci
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK
    J Mol Biol 306:329-47. 2001
    ..e. the various structural elements do not unfold simultaneously...
  6. ncbi request reprint Amyloid fibril formation by a helical cytochrome
    T A Pertinhez
    New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks, UK
    FEBS Lett 495:184-6. 2001
    ....
  7. ncbi request reprint Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy
    R Wijesinha-Bettoni
    Oxford Centre for Molecular Sciences, University of Oxford, New Chemistry Laboratory South Parks Road, Oxford, OX1 3QT, UK
    J Mol Biol 307:885-98. 2001
    ..Rather, the conversion appears to involve local reorganisations of the structure in the vicinity of the Ca(2+)-binding site that are coupled to the intrinsic fluctuations in the protein structure...
  8. ncbi request reprint Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds
    C Redfield
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Nat Struct Biol 6:948-52. 1999
    ....
  9. ncbi request reprint Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    J Zurdo
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, South Parks Road, Oxford, OX1 3QH, UK
    J Mol Biol 311:325-40. 2001
    ..Moreover, different hydrogen bonding patterns related to the various aggregate morphologies can be distinguished by FTIR analysis...
  10. pmc A refined solution structure of hen lysozyme determined using residual dipolar coupling data
    H Schwalbe
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, Oxford OX1 3QT, England
    Protein Sci 10:677-88. 2001
    ....
  11. ncbi request reprint Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations
    L J Smith
    Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QR, England
    J Mol Biol 280:703-19. 1998
    ..The results suggest that this approach has an important role to play in aiding the interpretation of experimental data for conformationally disordered non-native states of proteins...
  12. pmc High-sensitivity fluorescence anisotropy detection of protein-folding events: application to alpha-lactalbumin
    D Canet
    Oxford Centre for Molecular Sciences, University of Oxford, New Chemistry Laboratory, Oxford OX1 3QT, United Kingdom
    Biophys J 80:1996-2003. 2001
    ....
  13. ncbi request reprint Three key residues form a critical contact network in a protein folding transition state
    M Vendruscolo
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, UK
    Nature 409:641-5. 2001
    ..This result reveals how a nucleation mechanism involving a small number of key residues can lead to folding of a polypeptide chain to its unique native-state structure...
  14. ncbi request reprint Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy
    Y O Kamatari
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, UK
    Eur J Biochem 268:1782-93. 2001
    ..NMR diffusion measurements demonstrate that the effective hydrodynamic radius of denatured lysozyme, and hence the global properties of the denatured ensemble, do not change detectably at high pressure...
  15. ncbi request reprint Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH
    L J Smith
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, England, UK
    Proteins 36:77-86. 1999
    ..These structural and dynamical changes might be representative of the early stages of the transition to the molten-globule state of the protein known to be formed under low pH conditions in solution...
  16. ncbi request reprint The folding process of hen lysozyme: a perspective from the 'new view'
    A Matagne
    Oxford Centre for Molecular Sciences, University of Oxford, UK
    Cell Mol Life Sci 54:363-71. 1998
    ....
  17. ncbi request reprint Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules
    R Wijesinha-Bettoni
    Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, UK
    J Mol Biol 312:261-73. 2001
    ..Taken together, these results suggest that there may be a number of ways of stabilising a given protein fold, and the specific manner that this is achieved for a particular protein is determined by details of its sequence...
  18. pmc Solid state 31P cross-polarization/magic angle sample spinning nuclear magnetic resonance of crystalline glycogen phosphorylase b
    J E Taguchi
    Oxford Centre for Molecular Sciences, University of Oxford, United Kingdom
    Biophys J 64:492-501. 1993
    ....
  19. ncbi request reprint Collapse and cooperativity in protein folding
    A D Miranker
    New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, UK
    Curr Opin Struct Biol 6:31-42. 1996
    ..Recent experiments shed light on these issues and their relationships to the pathways of protein folding...
  20. pmc Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
    A K Chamberlain
    Oxford Centre for Molecular Sciences, University of Oxford, New Chemistry Laboratory, Oxford OX1 3QT, UK
    Protein Sci 10:2525-30. 2001
    ..This finding indicates that it is the increased ability of the variants to access partially folded conformations, rather than intrinsic changes in their native state properties, that is the origin of their amyloidogenicity...
  21. ncbi request reprint Time-resolved biophysical methods in the study of protein folding
    K W Plaxco
    New Chemistry Laboratory, University of Oxford, UK
    Curr Opin Struct Biol 6:630-6. 1996
    ..Recent advances in these techniques, the use of novel methods of initiating refolding, and a convergence of theoretical and experimental approaches are leading to a detailed understanding of many aspects of the folding process...
  22. ncbi request reprint The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site
    R Wain
    Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QH, United Kingdom
    J Biol Chem 276:45813-7. 2001
    ..The properties of the apo state of C11A/C14A cytochrome c(552) reported here contrast strongly with those of mitochondrial cytochrome c whose apo state resembles a random coil under similar conditions...
  23. ncbi request reprint Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    F Chiti
    Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK
    Nat Struct Biol 6:1005-9. 1999
    ....