Peter J Steinbach

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc Filtering artifacts from lifetime distributions when maximizing entropy using a bootstrapped model
    Peter J Steinbach
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892, USA
    Anal Biochem 427:102-5. 2012
  2. pmc Water-exclusion and liquid-structure forces in implicit solvation
    Sergio A Hassan
    Center for Molecular Modeling, DCB CIT, National Institutes of Health, US DHHS, Bethesda, Maryland 20892, United States
    J Phys Chem B 115:14668-82. 2011
  3. ncbi request reprint Computer simulation of protein-ligand interactions: challenges and applications
    Sergio A Hassan
    Center for Molecular Modeling, Division of Computational Bioscience, Center for Information Technology, National Institutes of Health DHHS, Bethesda, MD 20892, USA
    Methods Mol Biol 305:451-92. 2005
  4. doi request reprint Design of drug-resistant alleles of type-III phosphatidylinositol 4-kinases using mutagenesis and molecular modeling
    Andras Balla
    Section on Molecular Signal Transduction, Center for Developmental Neuroscience, NICHD, National Institutes of Health, Bethesda, Maryland 20892 4510, USA
    Biochemistry 47:1599-607. 2008
  5. pmc Prediction of side-chain conformations on protein surfaces
    Zhexin Xiang
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892 5624, USA
    Proteins 66:814-23. 2007
  6. ncbi request reprint Exploring peptide energy landscapes: a test of force fields and implicit solvent models
    Peter J Steinbach
    Center for Molecular Modeling, National Institutes of Health, DHHS, Bethesda, Maryland 20892 5624, USA
    Proteins 57:665-77. 2004
  7. pmc Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding
    Peter J Steinbach
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biophys J 82:2244-55. 2002
  8. ncbi request reprint Biological effect of a novel mutation in the third leucine-rich repeat of human luteinizing hormone receptor
    Michael Yiu Kwong Leung
    Laboratory of Clinical Genomics, National Institute of Child Health and Human Development, National Institutes of Health, Building 49, Room 2A08, 49 Convent Drive, MSC 4429, Bethesda, Maryland 20892 4429, USA
    Mol Endocrinol 20:2493-503. 2006
  9. pmc Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence
    Benjamin Schuler
    Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Building 5, Room 104, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 102:2754-9. 2005
  10. pmc Identifying protein kinase target preferences using mass spectrometry
    Jacqueline Douglass
    National Institutes of Health, Bethesda, MD 20892 1603, USA
    Am J Physiol Cell Physiol 303:C715-27. 2012

Collaborators

Detail Information

Publications14

  1. pmc Filtering artifacts from lifetime distributions when maximizing entropy using a bootstrapped model
    Peter J Steinbach
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892, USA
    Anal Biochem 427:102-5. 2012
    ..despite the presence of increased noise. In a second example, ambiguity in the interpretation of Poisson kinetics in the presence of scattered excitation light is resolved by filtering the prior model...
  2. pmc Water-exclusion and liquid-structure forces in implicit solvation
    Sergio A Hassan
    Center for Molecular Modeling, DCB CIT, National Institutes of Health, US DHHS, Bethesda, Maryland 20892, United States
    J Phys Chem B 115:14668-82. 2011
    ..The current implementation is ~1.5 times slower than the gas-phase force field and exhibits good parallel performance...
  3. ncbi request reprint Computer simulation of protein-ligand interactions: challenges and applications
    Sergio A Hassan
    Center for Molecular Modeling, Division of Computational Bioscience, Center for Information Technology, National Institutes of Health DHHS, Bethesda, MD 20892, USA
    Methods Mol Biol 305:451-92. 2005
    ..The results of these relatively simple conformational searches underscore the importance of incorporating protein flexibility in simulations of protein-ligand interactions, even in the context of relatively rigid binding pockets...
  4. doi request reprint Design of drug-resistant alleles of type-III phosphatidylinositol 4-kinases using mutagenesis and molecular modeling
    Andras Balla
    Section on Molecular Signal Transduction, Center for Developmental Neuroscience, NICHD, National Institutes of Health, Bethesda, Maryland 20892 4510, USA
    Biochemistry 47:1599-607. 2008
    ..These studies should aid development of subtype-specific inhibitors of type-III PI4Ks and help to better understand the significance of localized PtdIns4P production by the various PI4Ks isoforms in specific cellular compartments...
  5. pmc Prediction of side-chain conformations on protein surfaces
    Zhexin Xiang
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892 5624, USA
    Proteins 66:814-23. 2007
    ..The root mean square deviations obtained for hydrogen-bonding surface side chains were 1.64 and 1.81 A, with and without consideration of crystal packing effects, respectively...
  6. ncbi request reprint Exploring peptide energy landscapes: a test of force fields and implicit solvent models
    Peter J Steinbach
    Center for Molecular Modeling, National Institutes of Health, DHHS, Bethesda, Maryland 20892 5624, USA
    Proteins 57:665-77. 2004
    ..The thousands of simulations reported here suggest that the prediction of protein structure might be improved by the simultaneous use of a CMAP-like description of the main chain and an EEF1-like description of the solvent...
  7. pmc Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding
    Peter J Steinbach
    Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892, USA
    Biophys J 82:2244-55. 2002
    ..Analysis of the folding of dihydrofolate reductase reveals six kinetic processes, one more than previously reported...
  8. ncbi request reprint Biological effect of a novel mutation in the third leucine-rich repeat of human luteinizing hormone receptor
    Michael Yiu Kwong Leung
    Laboratory of Clinical Genomics, National Institute of Child Health and Human Development, National Institutes of Health, Building 49, Room 2A08, 49 Convent Drive, MSC 4429, Bethesda, Maryland 20892 4429, USA
    Mol Endocrinol 20:2493-503. 2006
    ..This mutation might also affect an LHR-dimer interaction. Thus, the I114F mutation reduces ligand binding and signal transduction by the hLHR, and it is partially responsible for Leydig cell hypoplasia in the patient...
  9. pmc Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence
    Benjamin Schuler
    Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Building 5, Room 104, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 102:2754-9. 2005
    ....
  10. pmc Identifying protein kinase target preferences using mass spectrometry
    Jacqueline Douglass
    National Institutes of Health, Bethesda, MD 20892 1603, USA
    Am J Physiol Cell Physiol 303:C715-27. 2012
    ....
  11. pmc Eukaryotic RNases H1 act processively by interactions through the duplex RNA-binding domain
    Sergei A Gaidamakov
    Laboratory of Molecular Genetics, National Institute of Child Health and Human Development Bethesda, MD 20892, USA
    Nucleic Acids Res 33:2166-75. 2005
    ..In mitochondria, where RNase H1 is essential for DNA formation during embryogenesis, long hybrids may be involved in DNA replication...
  12. pmc The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis
    Xiaolan Qian
    Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Cancer Cell 16:246-58. 2009
    ..Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding...
  13. ncbi request reprint Mutation in the leucine-rich repeat C-flanking region of platelet glycoprotein Ib beta impairs assembly of von Willebrand factor receptor
    Jingrong Tang
    Unit on Pediatric Genetics, Laboratory of Clinical Genomics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA
    Thromb Haemost 92:75-88. 2004
    ....
  14. ncbi request reprint Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography
    Ruiai Chu
    Laboratory of Biochemistry, Building 37, Room 6114E, National Cancer Institute, NIH, Bethesda, MD 20892 4255, USA
    J Mol Biol 323:253-62. 2002
    ..These results suggest that the hydrophobic interactions in the core are not sufficient to dictate the selection and that the location of the cutting site of the protease also influences the selection of structures...