World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
64
Citations
16508
World Ranking
7968
National Ranking
2315

Biology and Biochemistry

D-Index
63
Citations
16462
World Ranking
10096
National Ranking
4418

Research.com Recognitions

  • 1997 - Member of the National Academy of Sciences
  • 1986 - Fellow of the Royal Society, United Kingdom

Overview

George H. Lorimer is affiliated with the University of Maryland, College Park in the United States. Their research spans several interconnected areas within biochemistry, genetics, and molecular biology, with particular emphasis on molecular biology and materials chemistry.

The scientist's research topics include:

  • Photosynthetic Processes and Mechanisms
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Bacterial biofilms and quorum sensing
  • Carbon and Quantum Dots Applications
  • Nanocluster Synthesis and Applications

Frequent coauthors who have contributed to their research include Reza A. Ghiladi, Hasan Bayram, Jun Wang, and Yaqian Xiao.

Their work has been published in a range of scientific journals, including:

  • ACS Biomaterials Science & Engineering
  • Proceedings of the National Academy of Sciences
  • Food Chemistry
  • Science Advances
  • Frontiers in Molecular Biosciences

Examples of recent papers authored or coauthored by George H. Lorimer are:

  • "Hydrothermally Derived Green Carbon Dots from Broccoli Water Extracts: Decreased Toxicity, Enhanced Free-Radical Scavenging, and Anti-Inflammatory Performance" (2023), ACS Biomaterials Science & Engineering
  • "Ribulose 1,5-bisphosphate carboxylase/oxygenase activates O 2 by electron transfer" (2020), Proceedings of the National Academy of Sciences
  • "Extraction of weak hydrophobic sulforaphane from broccoli by salting-out assisted hydrophobic deep eutectic solvent extraction" (2022), Food Chemistry
  • "Ubiquitin is a carbon dioxide-binding protein" (2021), Science Advances
  • "Friends in need: How chaperonins recognize and remodel proteins that require folding assistance" (2022), Frontiers in Molecular Biosciences

George H. Lorimer has been recognized by the broader scientific community with membership in the National Academy of Sciences, awarded in 1997, and was named a Fellow of the Royal Society in the United Kingdom in 1986.

Best Publications

  • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

    Pierre Goloubinoff;Anthony A. Gatenby;George H. Lorimer

  • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

    Pierre Goloubinoff;John T. Christeller;Anthony A. Gatenby;George H. Lorimer

  • The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications.

    G H Lorimer;M R Badger;T J Andrews

  • RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE-OXYGENASE

    Unknown

  • Mechanism of Rubisco: The Carbamate as General Base.

    Cleland Ww;Andrews Tj;Gutteridge S;Hartman Fc

  • Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

    Matthew J. Todd;Paul V. Viitanen;George H. Lorimer

  • Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

    Paul V. Viitanen;Thomas H. Lubben;Janet Reed;Pierre Goloubinoff

  • D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities.

    G H Lorimer;M R Badger;T J Andrews

  • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.

    J A Mendoza;E Rogers;G H Lorimer;P M Horowitz

  • The Carboxylation and Oxygenation of Ribulose 1,5-Bisphosphate: The Primary Events in Photosynthesis and Photorespiration

    Unknown

  • Chaperonin-Mediated Protein Folding

    Unknown

  • Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves.

    T. J. Andrews;G. H. Lorimer;N. E. Tolbert

  • Carbamate formation on the epsilon-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+.

    George H. Lorimer;Henry M. Miziorko

  • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

    George H. Lorimer

  • Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.

    Paul V. Viitanen;Anthony A. Gatenby;George H. Lorimer

  • Crystal structure of the active site of ribulose-bisphosphate carboxylase

    Inger Andersson;Stefan Knight;Gunter Schneider;Ylva Lindqvist

  • Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

    Matthew J. Todd;George H. Lorimer;D. Thirumalai

  • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase.

    Paul V. Viitanen;Gail K. Donaldson;George H. Lorimer;Thomas H. Lubben

  • Rubisco: structure, mechanisms, and prospects for improvement

    Unknown

  • Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.

    P V Viitanen;G H Lorimer;R Seetharam;R S Gupta

  • Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase.

    Murray R. Badger;George H. Lorimer

  • Symmetric complexes of GroE chaperonins as part of the functional cycle.

    Marion Schmidt;Kerstin Rutkat;Reinhard Rachel;Günter Pfeifer

  • Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

    Matthew J. Todd;Paul V. Viitanen;George H. Lorimer

  • Ribulosebisphosphate carboxylase: amino acid sequence of a peptide bearing the activator carbon dioxide.

    George H. Lorimer

Frequent Co-Authors

Ylva Lindqvist
Ylva Lindqvist Karolinska Institute
Pierre Goloubinoff
Pierre Goloubinoff University of Lausanne
D. Thirumalai
D. Thirumalai The University of Texas at Austin
Murray R. Badger
Murray R. Badger Australian National University
Rainer Jaenicke
Rainer Jaenicke University of Regensburg
C. Barry Osmond
C. Barry Osmond Australian National University
Bernard R. Brooks
Bernard R. Brooks National Institutes of Health
Gunter Schneider
Gunter Schneider Karolinska Institute
Johannes Buchner
Johannes Buchner Technical University of Munich
Birgit Vennesland
Birgit Vennesland University of Chicago

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