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Chemistry

D-Index
73
Citations
16727
World Ranking
5056
National Ranking
1575

Research.com Recognitions

  • 2011 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1975 - Fellow of Alfred P. Sloan Foundation

Overview

Frederick W. Dahlquist is affiliated with the University of California, Santa Barbara in the United States. Their research primarily spans the field of Biochemistry, Genetics and Molecular Biology, with particular emphasis on Molecular Biology, Computational Theory and Mathematics, Genetics, Endocrinology, and Infectious Diseases.

The main topics of Dahlquist's work include:

  • Receptor Mechanisms and Signaling
  • Computational Drug Discovery Methods
  • Gene Regulatory Network Analysis
  • Bacterial Genetics and Biotechnology
  • Vibrio bacteria research studies
  • Clostridium difficile and Clostridium perfringens research

Their recent publications feature studies on molecular and bacterial mechanisms. These include:

  • "Rational design to control the trade-off between receptor affinity and cooperativity," 2020, Proceedings of the National Academy of Sciences
  • "Proteolytic processing induces a conformational switch required for antibacterial toxin delivery," 2022, Nature Communications
  • "Author Correction: Proteolytic processing induces a conformational switch required for antibacterial toxin delivery," 2022, Nature Communications

Dahlquist has collaborated frequently with several researchers, including:

  • Nicholas L. Bartelli
  • Victor J. Passanisi
  • K. Michalska
  • Ki-Ho Song
  • Dinh Q. Nhan

Their work has been published predominantly in Nature Communications and Proceedings of the National Academy of Sciences, with multiple contributions to each venue.

Dahlquist was awarded fellowships by prominent institutions, including the American Association for the Advancement of Science (AAAS) in 2011 and the Alfred P. Sloan Foundation in 1975.

Best Publications

  • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance.

    D C Muchmore;L P McIntosh;C B Russell;D E Anderson

  • Polarization-Enhanced NMR Spectroscopy of Biomolecules in Frozen Solution

    Dennis A. Hall;Douglas C. Maus;Douglas C. Maus;Gary J. Gerfen;Gary J. Gerfen;Souheil J. Inati;Souheil J. Inati

  • Studying excited states of proteins by NMR spectroscopy

    Frans A.A. Mulder;Anthony Mittermaier;Bin Hon;Frederick W. Dahlquist

  • pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.

    Unknown

  • Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway

    Julie A. Gegner;Daniel R. Graham;Amy F. Roth;Frederick W. Dahlquist

  • Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy: Application to Asn and Gln Residues in a Cavity Mutant of T4 Lysozyme

    Frans A. A. Mulder;Nikolai R. Skrynnikov;Bin Hon;Frederick W. Dahlquist

  • Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme.

    S. Dao-Pin;D. E. Anderson;W. A. Baase;F. W. Dahlquist

  • Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins

    Lawrence P. McIntosh;Frederick W. Dahlquist

  • Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

    Guillaume Bouvignies;Pramodh Vallurupalli;D. Flemming Hansen;Bruno E. Correia;Bruno E. Correia

  • Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme

    Guoliang Yang;Ciro Cecconi;Walter A. Baase;Ingrid R. Vetter

  • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28

    Gary W. Daughdrill;Meggen S. Chadsey;Joyce E. Karlinsey;Kelly T. Hughes

  • Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA

    Julie A. Gegner;Frederick W. Dahlquist

  • Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme.

    Nikolai R. Skrynnikov;Frans A. A. Mulder;Bin Hon;Frederick W. Dahlquist

  • 2D and 3D NMR spectroscopy employing carbon-13/carbon-13 magnetization transfer by isotropic mixing. Spin system identification in large proteins

    Stephen W. Fesik;Hugh L. Eaton;Edward T. Olejniczak;Erik R. P. Zuiderweg

  • The Amide 15N Chemical Shift Tensors of Four Peptides Determined from 13C Dipole-Coupled Chemical Shift Powder Patterns

    Terrence G. Oas;Cynthia J. Hartzell;Frederick W. Dahlquist;Gary P. Drobny

  • An HNCA Pulse Scheme for the Backbone Assignment of 15N,13C,2H-Labeled Proteins: Application to a 37-kDa Trp Repressor-DNA Complex

    Toshio Yamazaki;Weontae Lee;Matthew Revington;Debra L. Mattiello

  • Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.

    Nikolai R Skrynnikov;Frederick W Dahlquist;Lewis E Kay

  • Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.

    Stephan Wilkens;Frederick W. Dahlquist;Lawrence P. McIntosh;Logan W. Donaldson

  • Structural basis for the attachment of a paramyxoviral polymerase to its template

    Richard L. Kingston;Damon J. Hamel;Frederick W. Dahlquist

  • Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.

    Terrence G. Oas;Lawrence P. McIntosh;Erin K. O'Shea;Frederick W. Dahlquist

  • Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product.

    Marilyn R. Kehry;Martha W. Bond;Michael W. Hunkapiller;Frederick W. Dahlquist

Frequent Co-Authors

Lawrence P. McIntosh
Lawrence P. McIntosh University of British Columbia
Lewis E. Kay
Lewis E. Kay University of Toronto
Brian W. Matthews
Brian W. Matthews University of Oregon
Frans A. A. Mulder
Frans A. A. Mulder Aarhus University
Melvin I. Simon
Melvin I. Simon California Institute of Technology
Norbert O. Reich
Norbert O. Reich University of California, Santa Barbara
Roderick A. Capaldi
Roderick A. Capaldi University of Oregon
Gary P. Drobny
Gary P. Drobny University of Washington
James A. Hoch
James A. Hoch Scripps Research Institute

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