World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
61
Citations
14825
World Ranking
11264
National Ranking
4879

Research.com Recognitions

  • 1985 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • DNA

John F. Hunt spends much of his time researching Biochemistry, Protein structure, Nucleotide, Stereochemistry and ATP-binding cassette transporter. As part of his studies on Biochemistry, John F. Hunt often connects relevant subjects like Biophysics. His Protein structure research is multidisciplinary, incorporating perspectives in Computational biology, Protein Data Bank, Cystic fibrosis transmembrane conductance regulator and Protein folding.

His Cystic fibrosis transmembrane conductance regulator study combines topics in areas such as Cyclic nucleotide-binding domain and Cell biology. He has researched Nucleotide in several fields, including Nucleic acid and Active site. He interconnects Transport protein and Transmembrane protein in the investigation of issues within Stereochemistry.

His most cited work include:

  • ATP Binding to the Motor Domain from an ABC Transporter Drives Formation of a Nucleotide Sandwich Dimer. (688 citations)
  • Protein production and purification. (655 citations)
  • Glycophorin A dimerization is driven by specific interactions between transmembrane alpha helices (410 citations)

What are the main themes of his work throughout his whole career to date?

John F. Hunt mostly deals with Biochemistry, Protein structure, Crystallography, Stereochemistry and Structural genomics. His study brings together the fields of Biophysics and Biochemistry. His Protein structure study integrates concerns from other disciplines, such as Transport protein, Plasma protein binding, Cyclic nucleotide-binding domain, Structural biology and Binding site.

The concepts of his Crystallography study are interwoven with issues in Protein tertiary structure and Nuclear magnetic resonance spectroscopy. The Stereochemistry study combines topics in areas such as Lyase, Cofactor, Active site, Dimer and Molecule. His Structural genomics research also works with subjects such as

  • Computational biology together with Genetics and Genomics,
  • Bioinformatics, which have a strong connection to Crystallization.

He most often published in these fields:

  • Biochemistry (48.21%)
  • Protein structure (23.81%)
  • Crystallography (18.45%)

What were the highlights of his more recent work (between 2010-2021)?

  • Biochemistry (48.21%)
  • Protein structure (23.81%)
  • Crystallography (18.45%)

In recent papers he was focusing on the following fields of study:

John F. Hunt focuses on Biochemistry, Protein structure, Crystallography, Genetics and Cell biology. His Biochemistry research integrates issues from In vivo and Solubility. His study in Protein structure is interdisciplinary in nature, drawing from both Plasma protein binding, ATP hydrolysis, Active site, Structural biology and Protein engineering.

His studies deal with areas such as Protein sequencing, Protein tertiary structure, Macromolecular crystallography and Epitope as well as Crystallography. His work carried out in the field of Genetics brings together such families of science as Computational biology and Data science. His Cell biology research is multidisciplinary, relying on both Biogenesis, Membrane protein and Ribosomal protein.

Between 2010 and 2021, his most popular works were:

  • Codon influence on protein expression in E. coli correlates with mRNA levels (239 citations)
  • The COMBREX Project: Design, Methodology, and Initial Results (135 citations)
  • Computational design of catalytic dyads and oxyanion holes for ester hydrolysis. (92 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

John F. Hunt spends much of his time researching Biochemistry, Protein structure, Stereochemistry, Crystallography and Genetics. Translation elongation, Elongation factor, Mutant, Escherichia coli and A-site are the primary areas of interest in his Biochemistry study. As a part of the same scientific family, John F. Hunt mostly works in the field of Protein structure, focusing on Protein engineering and, on occasion, Computational biology, Synthetic biology and Plasma protein binding.

His research in Stereochemistry intersects with topics in Molecule, Catalysis, Active site and Protein design. John F. Hunt combines subjects such as Dimer, Protomer, Site-directed spin labeling and Tetramer with his study of Crystallography. His work on Regulation of gene expression and Genomic databases is typically connected to Project design and Microbial Genes as part of general Genetics study, connecting several disciplines of science.

Best Publications

  • Protein production and purification.

    S Gräslund

  • ATP Binding to the Motor Domain from an ABC Transporter Drives Formation of a Nucleotide Sandwich Dimer.

    Paul C Smith;Nathan Karpowich;Linda Millen;Jonathan E Moody

  • Glycophorin A dimerization is driven by specific interactions between transmembrane alpha helices

    M.A. Lemmon;J.M. Flanagan;J.F. Hunt;B.D. Adair

  • Clinical Evaluation of an Acellular Allograft Dermal Matrix in Full-Thickness Burns

    David J Wainwright;Michael Madden;Arnold Luterman;John Hunt

  • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

    John F. Hunt;Arthur J. Weaver;Samuel J. Landry;Samuel J. Landry;Lila Gierasch;Lila Gierasch

  • Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

    Hal A Lewis;Sean G Buchanan;Stephen K Burley;Kris Conners

  • Codon influence on protein expression in E. coli correlates with mRNA levels

    Grégory Boël;Grégory Boël;Reka Letso;Helen Neely;W. Nicholson Price;W. Nicholson Price

  • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters.

    Jonathan E. Moody;Linda Millen;Derk Binns;John F. Hunt

  • Crystal Structures of the MJ1267 ATP Binding Cassette Reveal an Induced-Fit Effect at the ATPase Active Site of an ABC Transporter

    Nathan Karpowich;Oksana Martsinkevich;Linda Millen;Yu Ren Yuan

  • Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA

    John F. Hunt;Sevil Weinkauf;Lisa Henry;John J. Fak

  • The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter.

    Yu Ren Yuan;Saul Blecker;Oksana Martsinkevich;Linda Millen

  • Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and Structure

    Hal A. Lewis;Xun Zhao;Chi Wang;J. Michael Sauder

  • Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix.

    John F. Hunt;Parshuram Rath;Kenneth J. Rothschild;Donald M. Engelman

  • The structural basis of cyclic diguanylate signal transduction by PilZ domains

    Jordi Benach;Swarup S Swaminathan;Rita Tamayo;Samuel K Handelman

  • Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB.

    Bomina Yu;William C. Edstrom;Jordi Benach;Yoshitomo Hamuro

  • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein.

    W. Christian Wigley;Rhesa D. Stidham;Nathan M. Smith;John F. Hunt

  • A biophysical study of integral membrane protein folding.

    John F. Hunt;Thomas N. Earnest;Olaf Bousché;Krishna Kalghatgi

  • secD, a new gene involved in protein export in Escherichia coli.

    C Gardel;S Benson;J Hunt;S Michaelis

  • Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data

    W Nicholson Price;W Nicholson Price;Yang Chen;Samuel K Handelman;Samuel K Handelman;Helen Neely

  • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding.

    Nathan K. Karpowich;Hector H. Huang;Paul C. Smith;John F. Hunt

Frequent Co-Authors

Gaetano T. Montelione
Gaetano T. Montelione Rensselaer Polytechnic Institute
Rong Xiao
Rong Xiao Rutgers, The State University of New Jersey
Burkhard Rost
Burkhard Rost Technical University of Munich
Liang Tong
Liang Tong Columbia University
Marc Fontecave
Marc Fontecave Collège de France
Philip J. Thomas
Philip J. Thomas The University of Texas Southwestern Medical Center
David Baker
David Baker University of Washington
Thomas Szyperski
Thomas Szyperski University at Buffalo, State University of New York
Johann Deisenhofer
Johann Deisenhofer The University of Texas Southwestern Medical Center
Masayori Inouye
Masayori Inouye Rutgers, The State University of New Jersey

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