{"entity": "researcher", "timestamp": "2026-08-13T19:13:38.500Z", "family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "affiliations": ["Biochemistry and Structural Biology, Center for Molecular Protein Science, Department of Chemistry, Lund University, 221 00 Lund, Sweden"], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae"}}, "publications": [{"entity": "publication", "iuid": "3fe1414d1f404aa7868cec9204360adb", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3fe1414d1f404aa7868cec9204360adb.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3fe1414d1f404aa7868cec9204360adb"}}, "title": "Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15", "authors": [{"family": "Ebenwaldner", "given": "Carmen", "initials": "C", "orcid": "0000-0002-7919-2994", "researcher": {"href": "https://publications.scilifelab.se/researcher/e2aedf9747ff49eb904e353f28847b61.json"}}, {"family": "Garc\u00eda Saura", "given": "Antonio Gin\u00e9s", "initials": "AG"}, {"family": "Ekstr\u00f6m", "given": "Simon", "initials": "S", "orcid": "0000-0002-7694-285X", "researcher": {"href": "https://publications.scilifelab.se/researcher/6416b323664f4126b70067193d7b8347.json"}}, {"family": "Bernfur", "given": "Katja", "initials": "K", "orcid": "0000-0002-7927-9563", "researcher": {"href": "https://publications.scilifelab.se/researcher/4600cd5ea61b41e4ab9b85af90fb41b4.json"}}, {"family": "Moche", "given": "Martin", "initials": "M"}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}, {"family": "Cohen", "given": "Michael S", "initials": "MS", "orcid": "0000-0002-7636-4156", "researcher": {"href": "https://publications.scilifelab.se/researcher/352749e458584319ab9d870abec5d90f.json"}}, {"family": "Sch\u00fcler", "given": "Herwig", "initials": "H", "orcid": "0000-0003-4059-3501", "researcher": {"href": "https://publications.scilifelab.se/researcher/f49b25ddfc934f3ca41020c3f38c6bfc.json"}}], "type": "journal-article", "published": "2025-10-29", "journal": {"title": "Nat Commun", "issn": "2041-1723", "issn-l": "2041-1723", "volume": "16", "issue": "1", "pages": null}, "abstract": null, "doi": "10.1038/s41467-025-65315-9", "pmid": null, "labels": {"Structural Proteomics": "Collaborative"}, "xrefs": [], "notes": [], "created": "2024-11-27T17:26:39.850Z", "modified": "2025-11-26T16:30:32.588Z"}, {"entity": "publication", "iuid": "df0652c365514257b768c4ffb776a3f3", "links": {"self": {"href": "https://publications.scilifelab.se/publication/df0652c365514257b768c4ffb776a3f3.json"}, "display": {"href": "https://publications.scilifelab.se/publication/df0652c365514257b768c4ffb776a3f3"}}, "title": "Bacterial transcriptional repressor NrdR - a flexible multifactorial nucleotide sensor.", "authors": [{"family": "Rozman Grinberg", "given": "Inna", "initials": "I"}, {"family": "Bima\u00ef", "given": "Ornella", "initials": "O"}, {"family": "Shahid", "given": "Saher", "initials": "S"}, {"family": "Philipp", "given": "Lena", "initials": "L"}, {"family": "Mart\u00ednez-Carranza", "given": "Markel", "initials": "M"}, {"family": "Banerjee", "given": "Ipsita", "initials": "I"}, {"family": "Lundin", "given": "Daniel", "initials": "D"}, {"family": "Stenmark", "given": "P\u00e5l", "initials": "P", "orcid": "0000-0003-4777-3417", "researcher": {"href": "https://publications.scilifelab.se/researcher/d97eba9f5edf4d76a5259c4baa8366c5.json"}}, {"family": "Sj\u00f6berg", "given": "Britt-Marie", "initials": "BM"}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}], "type": "journal article", "published": "2025-06-00", "journal": {"title": "FEBS J.", "issn": "1742-4658", "volume": "292", "issue": "12", "pages": "3091-3112", "issn-l": "1742-464X"}, "abstract": "NrdR is a bacterial transcriptional repressor consisting of a zinc (Zn)-ribbon domain followed by an ATP-cone domain. Understanding its mechanism of action could aid the design of novel antibacterials. NrdR binds specifically to two \"NrdR boxes\" upstream of ribonucleotide reductase operons, of which Escherichia coli has three: nrdHIEF, nrdDG and nrdAB, in the last of which we identified a new box. We show that E. coli NrdR (EcoNrdR) has similar binding strength to all three sites when loaded with ATP plus deoxyadenosine triphosphate (dATP) or equivalent diphosphate combinations. No other combination of adenine nucleotides promotes binding to DNA. We present crystal structures of EcoNrdR-ATP-dATP and EcoNrdR-ADP-dATP, which are the first high-resolution crystal structures of an NrdR. We have also determined cryo-electron microscopy structures of DNA-bound EcoNrdR-ATP-dATP and novel filaments of EcoNrdR-ATP. Tetrameric forms of EcoNrdR involve alternating interactions between pairs of Zn-ribbon domains and ATP-cones. The structures reveal considerable flexibility in relative orientation of ATP-cones vs Zn-ribbon domains. The structure of DNA-bound EcoNrdR-ATP-dATP shows that significant conformational rearrangements between ATP-cones and Zn-ribbons accompany DNA binding while the ATP-cones retain the same relative orientation. In contrast, ATP-loaded EcoNrdR filaments show rearrangements of the ATP-cone pairs and sequester the DNA-binding residues of NrdR such that they are unable to bind to DNA. Our results, in combination with a previous structural and biochemical study, point to highly flexible EcoNrdR structures that, when loaded with the correct nucleotides, adapt to an optimal promoter-binding conformation.", "doi": "10.1111/febs.70037", "pmid": "40029022", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC12176259"}, {"db": "RefSeq", "key": "NP_414947.1"}], "notes": [], "created": "2025-11-24T10:53:44.358Z", "modified": "2025-11-24T10:53:44.475Z"}, {"entity": "publication", "iuid": "3100faff46cb445d8dae8195bbe80fb2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3100faff46cb445d8dae8195bbe80fb2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3100faff46cb445d8dae8195bbe80fb2"}}, "title": "Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding", "authors": [{"family": "Bimai", "given": "Ornella", "initials": "O", "orcid": "0000-0003-0562-7251", "researcher": {"href": "https://publications.scilifelab.se/researcher/9545ade4d51c4c4089d97eb74841deec.json"}}, {"family": "Banerjee", "given": "Ipsita", "initials": "I"}, {"family": "Rozman Grinberg", "given": "Inna", "initials": "I", "orcid": "0000-0003-3094-1998", "researcher": {"href": "https://publications.scilifelab.se/researcher/2d4a64db2f9544b2bde744b063dc5247.json"}}, {"family": "Huang", "given": "Ping", "initials": "P", "orcid": "0000-0002-7676-6905", "researcher": {"href": "https://publications.scilifelab.se/researcher/f6e89aa29dfb4e06bd4c1530183dd8fb.json"}}, {"family": "Hultgren", "given": "Lucas", "initials": "L"}, {"family": "Ekstr\u00f6m", "given": "Simon", "initials": "S", "orcid": "0000-0002-7694-285X", "researcher": {"href": "https://publications.scilifelab.se/researcher/6416b323664f4126b70067193d7b8347.json"}}, {"family": "Lundin", "given": "Daniel", "initials": "D", "orcid": "0000-0002-8779-6464", "researcher": {"href": "https://publications.scilifelab.se/researcher/227cc90e084348a193fee05eb23a6bf3.json"}}, {"family": "Sj\u00f6berg", "given": "Britt Marie", "initials": "BM", "orcid": "0000-0001-5953-3360", "researcher": {"href": "https://publications.scilifelab.se/researcher/fab276f213364c2eaa6fe3dc5c9b01ff.json"}}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}], "type": "journal-article", "published": "2024-07-05", "journal": {"title": "Elife", "issn": "2050-084X", "issn-l": "2050-084X", "volume": "12", "issue": null, "pages": null}, "abstract": null, "doi": "10.7554/elife.89292.4", "pmid": null, "labels": {"Cryo-EM": "Service", "Structural Proteomics": "Service"}, "xrefs": [], "notes": [], "created": "2023-11-26T08:28:54.746Z", "modified": "2025-10-25T10:14:48.910Z"}, {"entity": "publication", "iuid": "7da5a92f39cc4ce2a269162f66b0d2e7", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7da5a92f39cc4ce2a269162f66b0d2e7.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7da5a92f39cc4ce2a269162f66b0d2e7"}}, "title": "A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.", "authors": [{"family": "Rozman Grinberg", "given": "Inna", "initials": "I", "orcid": "0000-0003-3094-1998", "researcher": {"href": "https://publications.scilifelab.se/researcher/2d4a64db2f9544b2bde744b063dc5247.json"}}, {"family": "Mart\u00ednez-Carranza", "given": "Markel", "initials": "M", "orcid": "0000-0003-0192-9762", "researcher": {"href": "https://publications.scilifelab.se/researcher/0ad7db8205c847a5bf56843d600e5ce1.json"}}, {"family": "Bimai", "given": "Ornella", "initials": "O", "orcid": "0000-0003-0562-7251", "researcher": {"href": "https://publications.scilifelab.se/researcher/9545ade4d51c4c4089d97eb74841deec.json"}}, {"family": "Noua\u00efria", "given": "Ghada", "initials": "G"}, {"family": "Shahid", "given": "Saher", "initials": "S"}, {"family": "Lundin", "given": "Daniel", "initials": "D", "orcid": "0000-0002-8779-6464", "researcher": {"href": "https://publications.scilifelab.se/researcher/227cc90e084348a193fee05eb23a6bf3.json"}}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}, {"family": "Sj\u00f6berg", "given": "Britt-Marie", "initials": "BM", "orcid": "0000-0001-5953-3360", "researcher": {"href": "https://publications.scilifelab.se/researcher/fab276f213364c2eaa6fe3dc5c9b01ff.json"}}, {"family": "Stenmark", "given": "P\u00e5l", "initials": "P", "orcid": "0000-0003-4777-3417", "researcher": {"href": "https://publications.scilifelab.se/researcher/d97eba9f5edf4d76a5259c4baa8366c5.json"}}], "type": "journal article", "published": "2022-05-16", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "13", "issue": "1", "pages": "2700", "issn-l": "2041-1723"}, "abstract": "Ribonucleotide reductase (RNR) is an essential enzyme that catalyzes the synthesis of DNA building blocks in virtually all living cells. NrdR, an RNR-specific repressor, controls the transcription of RNR genes and, often, its own, in most bacteria and some archaea. NrdR senses the concentration of nucleotides through its ATP-cone, an evolutionarily mobile domain that also regulates the enzymatic activity of many RNRs, while a Zn-ribbon domain mediates binding to NrdR boxes upstream of and overlapping the transcription start site of RNR genes. Here, we combine biochemical and cryo-EM studies of NrdR from Streptomyces coelicolor to show, at atomic resolution, how NrdR binds to DNA. The suggested mechanism involves an initial dodecamer loaded with two ATP molecules that cannot bind to DNA. When dATP concentrations increase, an octamer forms that is loaded with one molecule each of dATP and ATP per monomer. A tetramer derived from this octamer then binds to DNA and represses transcription of RNR. In many bacteria - including well-known pathogens such as Mycobacterium tuberculosis - NrdR simultaneously controls multiple RNRs and hence DNA synthesis, making it an excellent target for novel antibiotics development.", "doi": "10.1038/s41467-022-30328-1", "pmid": "35577776", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-022-30328-1"}, {"db": "pmc", "key": "PMC9110341"}], "notes": [], "created": "2022-05-30T08:19:29.322Z", "modified": "2023-12-04T10:19:23.813Z"}, {"entity": "publication", "iuid": "d1dc64598ece4c11a249a879a91936c0", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d1dc64598ece4c11a249a879a91936c0.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d1dc64598ece4c11a249a879a91936c0"}}, "title": "Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy.", "authors": [{"family": "Hasan", "given": "Mahmudul", "initials": "M", "orcid": "0000-0002-1767-6440", "researcher": {"href": "https://publications.scilifelab.se/researcher/67859983152248efb9f5a0461b168273.json"}}, {"family": "Banerjee", "given": "Ipsita", "initials": "I"}, {"family": "Rozman Grinberg", "given": "Inna", "initials": "I", "orcid": "0000-0003-3094-1998", "researcher": {"href": "https://publications.scilifelab.se/researcher/2d4a64db2f9544b2bde744b063dc5247.json"}}, {"family": "Sj\u00f6berg", "given": "Britt-Marie", "initials": "BM", "orcid": "0000-0001-5953-3360", "researcher": {"href": "https://publications.scilifelab.se/researcher/fab276f213364c2eaa6fe3dc5c9b01ff.json"}}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}], "type": "journal article", "published": "2021-07-26", "journal": {"title": "Front Mol Biosci", "issn": "2296-889X", "volume": "8", "pages": "713608", "issn-l": "2296-889X"}, "abstract": "The essential enzyme ribonucleotide reductase (RNR) is highly regulated both at the level of overall activity and substrate specificity. Studies of class I, aerobic RNRs have shown that overall activity is downregulated by the binding of dATP to a small domain known as the ATP-cone often found at the N-terminus of RNR subunits, causing oligomerization that prevents formation of a necessary \u03b12\u03b22 complex between the catalytic (\u03b12) and radical generating (\u03b22) subunits. In some relatively rare organisms with RNRs of the subclass NrdAi, the ATP-cone is found at the N-terminus of the \u03b2 subunit rather than more commonly the \u03b1 subunit. Binding of dATP to the ATP-cone in \u03b2 results in formation of an unusual \u03b24 tetramer. However, the structural basis for how the formation of the active complex is hindered by such oligomerization has not been studied. Here we analyse the low-resolution three-dimensional structures of the separate subunits of an RNR from subclass NrdAi, as well as the \u03b14\u03b24 octamer that forms in the presence of dATP. The results reveal a type of oligomer not previously seen for any class of RNR and suggest a mechanism for how binding of dATP to the ATP-cone switches off catalysis by sterically preventing formation of the asymmetrical \u03b12\u03b22 complex.", "doi": "10.3389/fmolb.2021.713608", "pmid": "34381817", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "713608"}, {"db": "pmc", "key": "PMC8350387"}], "notes": [], "created": "2021-12-14T12:28:03.468Z", "modified": "2023-12-04T10:17:16.657Z"}, {"entity": "publication", "iuid": "b9f68057256344ef94247b9c27877ef2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/b9f68057256344ef94247b9c27877ef2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/b9f68057256344ef94247b9c27877ef2"}}, "title": "Entropy-Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C.", "authors": [{"family": "Wallerstein", "given": "Johan", "initials": "J"}, {"family": "Ekberg", "given": "Vilhelm", "initials": "V", "orcid": "0000-0002-2813-3564", "researcher": {"href": "https://publications.scilifelab.se/researcher/db6fc60ac41f4de8b6c59d0c92b0dc35.json"}}, {"family": "Ignjatovi\u0107", "given": "Majda Misini", "initials": "MM"}, {"family": "Kumar", "given": "Rohit", "initials": "R"}, {"family": "Caldararu", "given": "Octav", "initials": "O"}, {"family": "Peterson", "given": "Kristoffer", "initials": "K"}, {"family": "Wernersson", "given": "Sven", "initials": "S"}, {"family": "Brath", "given": "Ulrika", "initials": "U"}, {"family": "Leffler", "given": "Hakon", "initials": "H", "orcid": "0000-0003-4482-8945", "researcher": {"href": "https://publications.scilifelab.se/researcher/7ddf9521718b41aebe37583acb403fd6.json"}}, {"family": "Oksanen", "given": "Esko", "initials": "E"}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}, {"family": "Nilsson", "given": "Ulf J", "initials": "UJ", "orcid": "0000-0001-5815-9522", "researcher": {"href": "https://publications.scilifelab.se/researcher/5d23150eb03f42ae866d49ff331ebc79.json"}}, {"family": "Ryde", "given": "Ulf", "initials": "U", "orcid": "0000-0001-7653-8489", "researcher": {"href": "https://publications.scilifelab.se/researcher/c80c2663ccfb4573bd922cd627a85655.json"}}, {"family": "Akke", "given": "Mikael", "initials": "M", "orcid": "0000-0002-2395-825X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e36b418e03154b90a8722670bed9e81a.json"}}], "type": "journal article", "published": "2021-04-26", "journal": {"title": "JACS Au", "issn": "2691-3704", "volume": "1", "issue": "4", "pages": "484-500", "issn-l": null}, "abstract": "Molecular recognition is fundamental to biological signaling. A central question is how individual interactions between molecular moieties affect the thermodynamics of ligand binding to proteins and how these effects might propagate beyond the immediate neighborhood of the binding site. Here, we investigate this question by introducing minor changes in ligand structure and characterizing the effects of these on ligand affinity to the carbohydrate recognition domain of galectin-3, using a combination of isothermal titration calorimetry, X-ray crystallography, NMR relaxation, and computational approaches including molecular dynamics (MD) simulations and grid inhomogeneous solvation theory (GIST). We studied a congeneric series of ligands with a fluorophenyl-triazole moiety, where the fluorine substituent varies between the ortho, meta, and para positions (denoted O, M, and P). The M and P ligands have similar affinities, whereas the O ligand has 3-fold lower affinity, reflecting differences in binding enthalpy and entropy. The results reveal surprising differences in conformational and solvation entropy among the three complexes. NMR backbone order parameters show that the O-bound protein has reduced conformational entropy compared to the M and P complexes. By contrast, the bound ligand is more flexible in the O complex, as determined by 19F NMR relaxation, ensemble-refined X-ray diffraction data, and MD simulations. Furthermore, GIST calculations indicate that the O-bound complex has less unfavorable solvation entropy compared to the other two complexes. Thus, the results indicate compensatory effects from ligand conformational entropy and water entropy, on the one hand, and protein conformational entropy, on the other hand. Taken together, these different contributions amount to entropy-entropy compensation among the system components involved in ligand binding to a target protein.", "doi": "10.1021/jacsau.0c00094", "pmid": "34467311", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC8395690"}], "notes": [], "created": "2021-07-02T14:10:17.149Z", "modified": "2025-10-17T13:03:56.005Z"}, {"entity": "publication", "iuid": "fb550d649c9942b08fcb359114458b65", "links": {"self": {"href": "https://publications.scilifelab.se/publication/fb550d649c9942b08fcb359114458b65.json"}, "display": {"href": "https://publications.scilifelab.se/publication/fb550d649c9942b08fcb359114458b65"}}, "title": "Interplay between Conformational Entropy and Solvation Entropy in Protein-Ligand Binding.", "authors": [{"family": "Verteramo", "given": "Maria Luisa", "initials": "ML"}, {"family": "Stenstr\u00f6m", "given": "Olof", "initials": "O"}, {"family": "Ignjatovi\u0107", "given": "Majda Misini", "initials": "MM"}, {"family": "Caldararu", "given": "Octav", "initials": "O"}, {"family": "Olsson", "given": "Martin A", "initials": "MA"}, {"family": "Manzoni", "given": "Francesco", "initials": "F"}, {"family": "Leffler", "given": "Hakon", "initials": "H", "orcid": "0000-0003-4482-8945", "researcher": {"href": "https://publications.scilifelab.se/researcher/7ddf9521718b41aebe37583acb403fd6.json"}}, {"family": "Oksanen", "given": "Esko", "initials": "E"}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications.scilifelab.se/researcher/da2734243cdb4142be696e5a82e788ae.json"}}, {"family": "Nilsson", "given": "Ulf J", "initials": "UJ", "orcid": "0000-0001-5815-9522", "researcher": {"href": "https://publications.scilifelab.se/researcher/5d23150eb03f42ae866d49ff331ebc79.json"}}, {"family": "Ryde", "given": "Ulf", "initials": "U", "orcid": "0000-0001-7653-8489", "researcher": {"href": "https://publications.scilifelab.se/researcher/c80c2663ccfb4573bd922cd627a85655.json"}}, {"family": "Akke", "given": "Mikael", "initials": "M", "orcid": "0000-0002-2395-825X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e36b418e03154b90a8722670bed9e81a.json"}}], "type": "journal article", "published": "2019-02-06", "journal": {"title": "J. Am. Chem. Soc.", "issn": "1520-5126", "volume": "141", "issue": "5", "pages": "2012-2026", "issn-l": "0002-7863"}, "abstract": "Understanding the driving forces underlying molecular recognition is of fundamental importance in chemistry and biology. The challenge is to unravel the binding thermodynamics into separate contributions and to interpret these in molecular terms. Entropic contributions to the free energy of binding are particularly difficult to assess in this regard. Here we pinpoint the molecular determinants underlying differences in ligand affinity to the carbohydrate recognition domain of galectin-3, using a combination of isothermal titration calorimetry, X-ray crystallography, NMR relaxation, and molecular dynamics simulations followed by conformational entropy and grid inhomogeneous solvation theory (GIST) analyses. Using a pair of diastereomeric ligands that have essentially identical chemical potential in the unbound state, we reduced the problem of dissecting the thermodynamics to a comparison of the two protein-ligand complexes. While the free energies of binding are nearly equal for the R and S diastereomers, greater differences are observed for the enthalpy and entropy, which consequently exhibit compensatory behavior, \u0394\u0394 H\u00b0(R - S) = -5 \u00b1 1 kJ/mol and - T\u0394\u0394 S\u00b0(R - S) = 3 \u00b1 1 kJ/mol. NMR relaxation experiments and molecular dynamics simulations indicate that the protein in complex with the S-stereoisomer has greater conformational entropy than in the R-complex. GIST calculations reveal additional, but smaller, contributions from solvation entropy, again in favor of the S-complex. Thus, conformational entropy apparently dominates over solvation entropy in dictating the difference in the overall entropy of binding. This case highlights an interplay between conformational entropy and solvation entropy, pointing to both opportunities and challenges in drug design.", "doi": "10.1021/jacs.8b11099", "pmid": "30618244", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2020-01-07T11:38:34.172Z", "modified": "2025-10-17T13:03:58.191Z"}]}