Matthew J Cuneo

Summary

Affiliation: Duke University Medical Center
Country: USA

Publications

  1. pmc The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog
    Matthew J Cuneo
    The Institute for Biological Structure and Design and the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA
    BMC Struct Biol 8:20. 2008
  2. pmc Ligand-induced conformational changes in a thermophilic ribose-binding protein
    Matthew J Cuneo
    The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    BMC Struct Biol 8:50. 2008
  3. doi request reprint Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins
    Matthew J Cuneo
    Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
    J Mol Biol 389:157-66. 2009
  4. pmc Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold
    Matthew J Cuneo
    Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 284:33217-23. 2009
  5. pmc Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein
    Yaji Tian
    Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    Protein Sci 16:2240-50. 2007
  6. ncbi request reprint The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites
    Matthew J Cuneo
    The Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
    J Mol Biol 362:259-70. 2006
  7. pmc Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport
    Matthew J Cuneo
    Department of Biochemistry, Duke University, Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 283:32812-20. 2008
  8. pmc Identification of cognate ligands for the Escherichia coli phnD protein product and engineering of a reagentless fluorescent biosensor for phosphonates
    Shahir S Rizk
    Duke University Medical Center, Department of Biochemistry, Durham, NC 27710, USA
    Protein Sci 15:1745-51. 2006
  9. pmc Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms
    J Jefferson Smith
    Duke University Medical Center, Department of Biochemistry, Box 3711, Research Drive, 415 Nanaline Duke Building, Durham, NC 27710, USA
    Protein Sci 14:64-73. 2005

Collaborators

Detail Information

Publications9

  1. pmc The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog
    Matthew J Cuneo
    The Institute for Biological Structure and Design and the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA
    BMC Struct Biol 8:20. 2008
    ..Of particular interest are pairs of homologous structures that are structurally very similar, but differ significantly in thermal stability...
  2. pmc Ligand-induced conformational changes in a thermophilic ribose-binding protein
    Matthew J Cuneo
    The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    BMC Struct Biol 8:50. 2008
    ....
  3. doi request reprint Structural adaptations that modulate monosaccharide, disaccharide, and trisaccharide specificities in periplasmic maltose-binding proteins
    Matthew J Cuneo
    Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
    J Mol Biol 389:157-66. 2009
    ..We provide a model in which the energetics of long-range conformational equilibria controls subsite occupancy and ligand binding...
  4. pmc Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold
    Matthew J Cuneo
    Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 284:33217-23. 2009
    ..Semi-specific recognition, in which a molecular class rather than individual species is selected, provides an efficient solution for the uptake of complex mixtures...
  5. pmc Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein
    Yaji Tian
    Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
    Protein Sci 16:2240-50. 2007
    ..The immobilized protein retains its response after long-term storage at room temperature...
  6. ncbi request reprint The crystal structure of a thermophilic glucose binding protein reveals adaptations that interconvert mono and di-saccharide binding sites
    Matthew J Cuneo
    The Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
    J Mol Biol 362:259-70. 2006
    ..Comparison of ttGBP and MBP provides a clear example of structural adaptations by which the size of ligand binding sites can be controlled in the PBP super family...
  7. pmc Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport
    Matthew J Cuneo
    Department of Biochemistry, Duke University, Medical Center, Durham, North Carolina 27710, USA
    J Biol Chem 283:32812-20. 2008
    ....
  8. pmc Identification of cognate ligands for the Escherichia coli phnD protein product and engineering of a reagentless fluorescent biosensor for phosphonates
    Shahir S Rizk
    Duke University Medical Center, Department of Biochemistry, Durham, NC 27710, USA
    Protein Sci 15:1745-51. 2006
    ..Since MP is the final degradation product of many nerve agents, these PhnD conjugates can function as components in a biosensor system for chemical warfare agents...
  9. pmc Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms
    J Jefferson Smith
    Duke University Medical Center, Department of Biochemistry, Box 3711, Research Drive, 415 Nanaline Duke Building, Durham, NC 27710, USA
    Protein Sci 14:64-73. 2005
    ..Together, these experiments demonstrated that reversible thiol protection schemes provide a rapid, straightforward method for producing multiple, site-specific modifications...