G
Glen E. Kellogg
Researcher at Virginia Commonwealth University
Publications - 152
Citations - 5494
Glen E. Kellogg is an academic researcher from Virginia Commonwealth University. The author has contributed to research in topics: Ligand (biochemistry) & Chemistry. The author has an hindex of 44, co-authored 143 publications receiving 5061 citations. Previous affiliations of Glen E. Kellogg include VCU Medical Center & Northwestern University.
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Journal ArticleDOI
HINT: A new method of empirical hydrophobic field calculation for CoMFA
TL;DR: An empirical hydrophobic field-like 3D function has been calculated with the program HINT (hydrophobic interactions) and imported into the SYBYL implementation of CoMFA (Comparative Molecular Field Analysis).
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Target flexibility: an emerging consideration in drug discovery and design.
Pietro Cozzini,Glen E. Kellogg,Francesca Spyrakis,Donald J. Abraham,Gabriele Costantino,Andrew Emerson,Francesca Fanelli,Holger Gohlke,Leslie A. Kuhn,Garrett M. Morris,Modesto Orozco,Thelma A. Pertinhez,Menico Rizzi,Christoph A. Sotriffer +13 more
TL;DR: Department of General and Inorganic Chemistry, UniVersity of Parma, Via G.P. Usberti 17/A 43100, Parma; Department of Medicinal Chemistry and Institute for Structural Biology & Drug DiscoVery, Virginia Commonwealth Uni Versity, Richmond, Virginia 23298-0540.
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Hydrophobicity: is LogPo/w more than the sum of its parts?
TL;DR: In this article, an empirically calculated parameter LogPo/w, the log10 of the coefficient for solvent partitioning between 1-octanol and water, has been used to provide the key data for a unique non-covalent interaction force field called HINT (Hydropathic INTeractions).
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Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water.
Pietro Cozzini,Micaela Fornabaio,Anna Marabotti,Donald J. Abraham,Glen E. Kellogg,Andrea Mozzarelli +5 more
TL;DR: A relatively simple and intuitive calculation procedure for estimating the free energy of binding for 53 protein-ligand complexes formed by 17 proteins of known three-dimensional structure and characterized by different active site polarity is described.
Journal ArticleDOI
Allosteric modifiers of hemoglobin. 2. Crystallographically determined binding sites and hydrophobic binding/interaction analysis of novel hemoglobin oxygen effectors.
TL;DR: The protein-bound conformations of six new allosteric effectors similar to bezafibrate that markedly decrease the oxygen affinity of hemoglobin have been determined by X-ray crystallography.