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William F. DeGrado

Researcher Next ID · RN-026362

Researcher · Biochemistry, Genetics and Molecular Biology

University of California, San Francisco

San Francisco, Japan

Not currently recruitingFunding unknown
Works count
756
Citation count
53,772
H-index
125
i10-index
493

Research interests

Biochemistry, Genetics and Molecular Biology
Medicine
Protein Structure and Dynamics
Chemical Synthesis and Analysis
RNA and protein synthesis mechanisms
Lipid Membrane Structure and Behavior
Cell Adhesion Molecules Research

Publications

  • Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity

    Nature Communications · 2017 · 10.1038/s41467-017-01447-x

  • Short peptides self-assemble to produce catalytic amyloids

    Nature Chemistry · 2014 · https://doi.org/10.1038/nchem.1894

  • Salt bridges: Geometrically specific, designable interactions

    Proteins Structure Function and Bioinformatics · 2010 · 10.1002/prot.22927

  • Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

    Nature · 2010 · 10.1038/nature08722

  • De Novo Design of Antimicrobial Polymers, Foldamers, and Small Molecules: From Discovery to Practical Applications

    Accounts of Chemical Research · 2009 · 10.1021/ar900036b

  • The Role of Hydrophobicity in the Antimicrobial and Hemolytic Activities of Polymethacrylate Derivatives

    Chemistry - A European Journal · 2008 · 10.1002/chem.200801523

  • Structural basis for the function and inhibition of an influenza virus proton channel

    Nature · 2008 · 10.1038/nature06528

  • Foldamers as versatile frameworks for the design and evolution of function

    Nature Chemical Biology · 2007 · https://doi.org/10.1038/nchembio876

  • Amphiphilic Polymethacrylate Derivatives as Antimicrobial Agents

    Journal of the American Chemical Society · 2005 · 10.1021/ja044205+

  • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs

    Current Opinion in Structural Biology · 2004 · 10.1016/j.sbi.2004.07.007

  • Using Nitrile-Derivatized Amino Acids as Infrared Probes of Local Environment

    Journal of the American Chemical Society · 2002 · 10.1021/ja0285262

  • De novo design of biomimetic antimicrobial polymers

    Proceedings of the National Academy of Sciences · 2002 · 10.1073/pnas.082046199

  • β-Peptides: From Structure to Function

    Chemical Reviews · 2001 · https://doi.org/10.1021/cr000045i

  • Asparagine-mediated self-association of a model transmembrane helix.

    Nature Structural Biology · 2000 · 10.1038/72440

  • De Novo Design and Structural Characterization of Proteins and Metalloproteins

    Annual Review of Biochemistry · 1999 · 10.1146/annurev.biochem.68.1.779

  • De Novo Design of Antibacterial β-Peptides

    Journal of the American Chemical Society · 1999 · 10.1021/ja992728p

  • The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure

    Proceedings of the National Academy of Sciences · 1999 · 10.1073/pnas.96.5.2036

  • A functionally defined model for the M 2 proton channel of influenza A virus suggests a mechanism for its ion selectivity

    Proceedings of the National Academy of Sciences · 1997 · 10.1073/pnas.94.21.11301

  • Protein Design: A Hierarchic Approach

    Science · 1995 · 10.1126/science.270.5238.935

  • Design and synthesis of multi-haem proteins

    Nature · 1994 · 10.1038/368425a0

  • A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids

    Science · 1990 · https://doi.org/10.1126/science.2237415

  • How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices

    Trends in Biochemical Sciences · 1990 · https://doi.org/10.1016/0968-0004(90)90177-d

  • Protein Design, a Minimalist Approach

    Science · 1989 · 10.1126/science.2464850

  • Characterization of a Helical Protein Designed from First Principles

    Science · 1988 · 10.1126/science.3043666

  • Induction of peptide conformation at apolar water interfaces. 1. A study with model peptides of defined hydrophobic periodicity

    Journal of the American Chemical Society · 1985 · 10.1021/ja00311a076

Current projects

    No projects listed.