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binding sites (8) 8
biochemistry & molecular biology (8) 8
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biophysics (7) 7
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ligands (7) 7
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amino acid sequence (4) 4
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nmr (4) 4
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backbone amide (3) 3
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studies (3) 3
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base sequence (2) 2
bile acids and salts - chemical synthesis (2) 2
bile acids and salts - chemistry (2) 2
biochemistry (2) 2
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blood (2) 2
calcium-binding proteins - chemistry (2) 2
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drosophila proteins - chemistry (2) 2
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genotype & phenotype (2) 2
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guanidine (2) 2
histoplasma capsulatum (2) 2
hydroxylation (2) 2
hydroxysteroid dehydrogenases (2) 2
hydroxysteroid dehydrogenases - metabolism (2) 2
ileum - metabolism (2) 2
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1. Full Text Interchange of L-, Z-, and Bound-Ion-Pair X-Type Ligation on Cadmium Selenide Quantum Belts
by Yao, Yuewei and DeKoster, Gregory T and Buhro, William E
Chemistry of Materials, ISSN 0897-4756, 06/2019, Volume 31, Issue 11, pp. 4299 - 4312
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2. Full Text Antiparallel EmrE exports drugs by exchanging between asymmetric structures
by Morrison, Emma A and Dekoster, Gregory T and Dutta, Supratik and Vafabakhsh, Reza and Clarkson, Michael W and Bahl, Arjun and Kern, Dorothee and Ha, Taekjip and Henzler-Wildman, Katherine A
Nature, ISSN 0028-0836, 01/2012, Volume 481, Issue 7379, pp. 45 - 52
Small multidrug resistance transporters provide an ideal system to study the minimal requirements for active transport. EmrE is one such transporter in... 
CONFORMATIONAL-CHANGES | SUBSTRATE-BINDING | LIGAND-BINDING | PROTON RELEASE | MECHANISM | MULTIDRUG TRANSPORTER EMRE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | STATE | MODEL | MEMBRANE TOPOLOGY | Catalytic Domain | Antiporters - chemistry | Protein Multimerization | Models, Molecular | Antiporters - metabolism | Escherichia coli Proteins - metabolism | Escherichia coli - chemistry | Pharmaceutical Preparations - metabolism | Biological Transport | Escherichia coli - metabolism | Water - chemistry | Fluorescence Resonance Energy Transfer | Nuclear Magnetic Resonance, Biomolecular | Protein Conformation | Escherichia coli Proteins - chemistry | Usage | Escherichia coli | Biological transport, Active | Nuclear magnetic resonance spectroscopy | Research | Drug resistance | Properties | Lipids | Asymmetry | Experiments | Spectrum analysis | Symmetry
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3. A Compare-and-Contrast NMR Dynamics Study of Two Related RRMs: U1A and SNF
by Gregory T DeKoster and Kimberly J Delaney and Kathleen B Hall
Biophysical Journal, ISSN 0006-3495, 07/2014, Volume 107, Issue 1, p. 208
  The U1A/U2B"/SNF family of small nuclear ribonucleoproteins uses a phylogenetically conserved RNA recognition motif (RRM1) to bind RNA stemloops in U1 and/or... 
Proteins | Insects | Phylogenetics | Ribonucleic acid--RNA | Binding sites
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4. Full Text Red Blood Cell Invasion by Plasmodium vivax: Structural Basis for DBP Engagement of DARC
by Batchelor, Joseph D and Malpede, Brian M and Omattage, Natalie S and DeKoster, Gregory T and Henzler-Wildman, Katherine A and Tolia, Niraj H
PLoS Pathogens, ISSN 1553-7366, 01/2014, Volume 10, Issue 1, p. e1003869
Plasmodium parasites use specialized ligands which bind to red blood cell (RBC) receptors during invasion. Defining the mechanism of receptor recognition is... 
RECOGNITION | FALCIPARUM | CHEMOKINES | ANTIGEN/RECEPTOR | MICROBIOLOGY | DUFFY-BINDING-PROTEIN | LIGAND DOMAIN | VIROLOGY | MALARIA | RESIDUES | RECEPTOR-BINDING | PARASITOLOGY | ANTIGEN | Antigens, Protozoan - immunology | Malaria, Vivax - genetics | Humans | Structure-Activity Relationship | Erythrocytes - chemistry | Protozoan Proteins - genetics | Protozoan Proteins - chemistry | Receptors, Cell Surface - chemistry | Antigens, Protozoan - genetics | Duffy Blood-Group System - immunology | Plasmodium vivax - chemistry | Erythrocytes - immunology | Cell Line | Plasmodium vivax - metabolism | Antigens, Protozoan - chemistry | Plasmodium vivax - immunology | Receptors, Cell Surface - immunology | Point Mutation | Immune Evasion | Protein Binding | Malaria, Vivax - immunology | Duffy Blood-Group System - genetics | Erythrocytes - parasitology | Protozoan Proteins - immunology | Duffy Blood-Group System - chemistry | Receptors, Cell Surface - genetics | Plasmodium | Antigens | Microbiological research | Erythrocytes | Host-parasite relationships | Research | Health aspects | Binding sites (Biochemistry) | Proteins | Studies | Genotype & phenotype | Biomedical research | Ligands | Parasites | Binding sites | Blood | Chemokines
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5. Full Text Molecular principles underlying dual RNA specificity in the Drosophila SNF protein
by Weber, Gert and Dekoster, Gregory T and Holton, Nicole and Hall, Kathleen B and Wahl, Markus C
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 2220 - 16
The first RNA recognition motif of the Drosophila SNF protein is an example of an RNA binding protein with multi-specificity. It binds different RNA hairpin... 
MOTIFS | DOMAIN | RECOGNITION | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | BINDING PROTEINS | RESOLUTION | DYNAMICS | IDENTIFICATION | Ribonucleoprotein, U1 Small Nuclear - metabolism | Ribonucleoprotein, U2 Small Nuclear - chemistry | Substrate Specificity - physiology | Crystallography, X-Ray | Drosophila Proteins - metabolism | Ribonucleoprotein, U1 Small Nuclear - isolation & purification | Recombinant Proteins - isolation & purification | Protein Domains - physiology | Ribonucleoprotein, U2 Small Nuclear - metabolism | Ribonucleoprotein, U1 Small Nuclear - chemistry | Nuclear Magnetic Resonance, Biomolecular | Recombinant Proteins - metabolism | Mutagenesis, Site-Directed | Models, Molecular | Recombinant Proteins - chemistry | Ribonucleoprotein, U1 Small Nuclear - genetics | Recombinant Proteins - genetics | Binding Sites - genetics | Drosophila Proteins - chemistry | Drosophila Proteins - isolation & purification | Amino Acid Motifs - physiology | RNA, Small Nuclear - chemistry | Drosophila Proteins - genetics | RNA, Small Nuclear - metabolism | Amino Acid Motifs - genetics | Protein Binding - physiology | Dynamic structural analysis | Drosophila | Base pairs | Ribonucleic acid--RNA | Molecular chains | Proteins | Magnetic resonance spectroscopy | RNA-binding protein | Mutagenesis | Insects | Affinity | NMR spectroscopy | Crystal structure | Tips
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6. Full Text Structural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR
by Horváth, Gergő and Bencsura, Ákos and Simon, Ágnes and Tochtrop, Gregory P and DeKoster, Gregory T and Covey, Douglas F and Cistola, David P and Toke, Orsolya
The FEBS Journal, ISSN 1742-464X, 02/2016, Volume 283, Issue 3, pp. 541 - 555
Besides aiding digestion, bile salts are important signal molecules exhibiting a regulatory role in metabolic processes. Human ileal bile acid binding protein... 
molecular recognition | cooperativity | conformational selection | enterohepatic circulation | lipid binding proteins | RAT | BIOCHEMISTRY & MOLECULAR BIOLOGY | SITE SELECTIVITY | SALTS | BACKBONE AMIDE | HELICAL DOMAIN | SIDE-CHAIN RESONANCES | FATTY-ACID | DYNAMICS | C-13-LABELED PROTEINS | Glycocholic Acid - chemistry | Hydrogen Bonding | Magnetic Resonance Spectroscopy | Solutions | Humans | Membrane Glycoproteins - chemistry | Hydrophobic and Hydrophilic Interactions | Carrier Proteins - chemistry | Ligands | Molecular Structure | Binding Sites | Glycochenodeoxycholic Acid - chemistry | Chemical properties | Nuclear magnetic resonance | Binding proteins | Hydrogen | Protein binding | Deoxycholic acid | Proteins | Rodents | Bile
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7. Full Text ApoE: In Vitro Studies of a Small Molecule Effector
by Mondal, Tridib and Wang, Hanliu and DeKoster, Gregory T and Baban, Berevan and Gross, Michael L and Frieden, Carl
Biochemistry, ISSN 0006-2960, 05/2016, Volume 55, Issue 18, pp. 2613 - 2621
Apolipoprotein E4 (apoE4), one of three isoforms of apoE, is the major risk factor for developing late onset Alzheimer’s disease. The only differences among... 
LIPOPROTEIN | STRUCTURAL DIFFERENCES | FLUORESCENCE ANALYSIS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN APOLIPOPROTEIN-E | HYDROGEN/DEUTERIUM EXCHANGE | PROTEIN-LIGAND INTERACTIONS | HEPARIN-BINDING-SITES | MASS-SPECTROMETRY | Lipoproteins, LDL - chemistry | Apolipoprotein E4 - metabolism | Humans | Alzheimer Disease - drug therapy | Receptors, LDL - metabolism | Apolipoprotein E4 - antagonists & inhibitors | Receptors, LDL - chemistry | Deuterium Exchange Measurement | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Alzheimer Disease - metabolism | Protein Domains | Lipoproteins, LDL - metabolism | Apolipoprotein E4 - chemistry | Heparin - chemistry | Protein Isoforms - antagonists & inhibitors | Fertilization in vitro | Molecular weights | Usage | Apolipoproteins | Analysis
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8. Full Text A Compare-and-Contrast NMR Dynamics Study of Two Related RRMs: U1A and SNF
by DeKoster, Gregory T and Delaney, Kimberly J and Hall, Kathleen B
Biophysical Journal, ISSN 0006-3495, 07/2014, Volume 107, Issue 1, pp. 208 - 219
The U1A/U2B″/SNF family of small nuclear ribonucleoproteins uses a phylogenetically conserved RNA recognition motif (RRM1) to bind RNA stemloops in U1 and/or... 
COLLECTIVE ATOMIC FLUCTUATIONS | MOLECULAR-DYNAMICS | A-PROTEIN | BIOPHYSICS | CRYSTAL-STRUCTURE | CONFORMATIONAL CAPTURE | RNA-BINDING DOMAIN | U1A-RNA COMPLEX | INDUCED FIT | DROSOPHILA-SNF | RBD1 PROTEIN | Ribonucleoprotein, U1 Small Nuclear - metabolism | Amino Acid Sequence | Magnetic Resonance Spectroscopy | Drosophila - chemistry | Molecular Sequence Data | Ribonucleoprotein, U1 Small Nuclear - genetics | Drosophila Proteins - chemistry | Drosophila Proteins - metabolism | Animals | Base Sequence | Ribonucleoprotein, U1 Small Nuclear - chemistry | Protein Binding | RNA, Small Nuclear - chemistry | Molecular Docking Simulation | Drosophila - metabolism | Drosophila Proteins - genetics | Mutation | RNA, Small Nuclear - metabolism | Binding Sites | Thermodynamics | Nuclear magnetic resonance | Phenylalanine | RNA | Molecular biology | Glutamine | Binding | Residues | Ribonucleic acids | Dynamics | Amino acids | Nanostructure | Dispersions | Proteins and Nucleic Acids
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9. Full Text Mechanistic Investigations into the Multi-Drug Resistance Transporter, EmrE
by Morrison, Emma A and DeKoster, Gregory T and Liu, Yongjia and Henzler-Wildman, Katherine A
Biophysical Journal, ISSN 0006-3495, 01/2012, Volume 102, Issue 3, pp. 215a - 215a
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10. Full Text Red Blood Cell Invasion by Plasmodium vivax: Structural Basis for DBP Engagement of DARC
: e1003869
by Joseph D Batchelor and Brian M Malpede and Natalie S Omattage and Gregory T DeKoster and Katherine A Henzler-Wildman and Niraj H Tolia
PLoS Pathogens, ISSN 1553-7366, 01/2014, Volume 10, Issue 1
  Plasmodium parasites use specialized ligands which bind to red blood cell (RBC) receptors during invasion. Defining the mechanism of receptor recognition is... 
Proteins | Studies | Antigens | Genotype & phenotype | Biomedical research | Erythrocytes | Ligands | Parasites | Binding sites | Blood | Chemokines
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11. Full Text NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
by Beck, Moriah R and DeKoster, Gregory T and Cistola, David P and Goldman, William E
Molecular Microbiology, ISSN 0950-382X, 04/2009, Volume 72, Issue 2, pp. 344 - 353
Summary The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on... 
MEMBRANE INTERACTIONS | SPHINGOLIPID ACTIVATOR PROTEINS | AMBIGUOUS DISTANCE RESTRAINTS | CRYSTAL-STRUCTURE | AUTOMATED ASSIGNMENT | BIOCHEMISTRY & MOLECULAR BIOLOGY | MICROBIOLOGY | NK-LYSIN | INTRACELLULAR PARASITISM | CALCIUM-DEPENDENCE | BACTERIOCIN AS-48 | HISTOPLASMA-CAPSULATUM | Calcium-Binding Proteins - chemistry | Fungal Proteins - chemistry | Amino Acid Sequence | Saposins - chemistry | Models, Molecular | Molecular Sequence Data | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | Histoplasma - chemistry | Protein Conformation | Virulence Factors - chemistry | Dimerization | Plant lipids | Nuclear magnetic resonance | Glycolipids | Analysis | Monomers | Protein binding | phagolysosome | Histoplasma capsulatum | structural homology | lipid binding
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12. Full Text Determinants of Cooperativity and Site Selectivity in Human Ileal Bile Acid Binding Protein
by Toke, Orsolya and Monsey, John D and DeKoster, Gregory T and Tochtrop, Gregory P and Tang, Changguo and Cistola, David P
Biochemistry, ISSN 0006-2960, 01/2006, Volume 45, Issue 3, pp. 727 - 737
Human ileal bile acid binding protein (I-BABP) is a member of the family of intracellular lipid-binding proteins and is thought to play a role in the... 
BACKBONE AMIDE | NMR | MUTAGENESIS | C-13 | SPECTROSCOPY | SIDE-CHAIN RESONANCES | BIOCHEMISTRY & MOLECULAR BIOLOGY | SECONDARY STRUCTURE | LARGER PROTEINS | IDENTIFICATION | C-13-LABELED PROTEINS | Humans | Ileum - metabolism | Isotope Labeling | Models, Molecular | Protein Binding | Substrate Specificity | Bile Acids and Salts - metabolism | Hydroxysteroid Dehydrogenases - metabolism | Protein Conformation | Kinetics | Binding Sites
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13. Full Text A Single Hydroxyl Group Governs Ligand Site Selectivity in Human Ileal Bile Acid Binding Protein
by Tochtrop, Gregory P and DeKoster, Gregory T and Covey, Douglas F and Cistola, David P
Journal of the American Chemical Society, ISSN 0002-7863, 09/2004, Volume 126, Issue 35, pp. 11024 - 11029
The recognition between proteins and their native ligands is fundamental to biological function. In vivo, human ileal bile acid binding protein (I-BABP)... 
SENSITIVITY | CHEMISTRY, MULTIDISCIPLINARY | NMR | Recombinant Proteins - metabolism | Hydroxysteroid Dehydrogenases - chemistry | Humans | Ileum - chemistry | Ileum - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Structure-Activity Relationship | Hydroxysteroid Dehydrogenases - genetics | Escherichia coli - genetics | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Hydroxysteroid Dehydrogenases - metabolism | Ligands | Binding Sites | Bile acids | Urinary diversion | Research | Hydroxylation | Methods
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14. NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
by Moriah R Beck and Gregory T DeKoster and David P Cistola and William E Goldman
Molecular Microbiology, ISSN 0950-382X, 04/2009, Volume 72, Issue 2, p. 344
The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its... 
Fungi | Nuclear magnetic resonance--NMR | Bacterial proteins | Lipids | Binding sites | Virology
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15. Full Text The RXRα C-terminus T462 is a NMR sensor for coactivator peptide binding
by Lu, Jianyun and Chen, Minghe and DeKoster, Gregory T and Cistola, David P and Li, Ellen
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2008, Volume 366, Issue 4, pp. 932 - 937
The C-terminal activation function-2 (AF-2) helix plays a crucial role in retinoid X receptor alpha (RXRα)-mediated gene expression. Here, we report a nuclear... 
Coactivator | GRIP1 | NMR | Activation | RXRα | Isothermal titration calorimetry | DOMAIN | ACTIVATED RECEPTOR-GAMMA | LIGAND-BINDING | BIOLOGICAL MACROMOLECULES | PROTEIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | RETINOIC-ACID | ANISOTROPY | isothermal titration calorimetry | BIOPHYSICS | RXR alpha | activation | coactivator
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16. Full Text Palladium-Catalyzed Potassium Enoxyborate Alkylation of Enantiopure Hajos−Parrish Indenone To Construct Rearranged Steroid Ring Systems
by Jastrzebska, Izabella and Scaglione, Jamie B and DeKoster, Gregory T and Rath, Nigam P and Covey, Douglas F
The Journal of Organic Chemistry, ISSN 0022-3263, 06/2007, Volume 72, Issue 13, pp. 4837 - 4843
Here we report the stereo- and regiospecific C-6 alkylation of a trans-inden-5-one (from optically pure Hajos−Parrish ketone) with allylic electrophiles. Use... 
CARBON BOND FORMATION | CHEMISTRY, ORGANIC | TRANSITION-METAL CATALYSIS | ALLYLATION | ANALOGUES | Anthracenes - chemistry | Benzene - chemistry | Molecular Structure | Catalysis | Borates - chemistry | Indenes - chemistry | Palladium - chemistry | Alkylation | Steroids - chemistry
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17. Full Text Structural Features Responsible for the Biological Stability of Histoplasma’s Virulence Factor CBP
by Beck, Moriah R and DeKoster, Gregory T and Hambly, David M and Gross, Michael L and Cistola, David P and Goldman, William E
Biochemistry, ISSN 0006-2960, 04/2008, Volume 47, Issue 15, pp. 4427 - 4438
The virulence factor CBP is the most abundant protein secreted by Histoplasma capsulatum, a pathogenic fungus that causes histoplasmosis. Although the... 
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18. Full Text Structural Features Responsible for the Biological Stability ofHistoplasma’s Virulence Factor CBP
by Beck, Moriah R and DeKoster, Gregory T and Hambly, David M and Gross, Michael L and Cistola, David P and Goldman, William E
Biochemistry, ISSN 0006-2960, 04/2008, Volume 47, Issue 15, pp. 4427 - 4438
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19. Full Text Structural features responsible for the biological stability of Histoplasma's virulence factor CBP
by Beck, Moriah R and DeKoster, Gregory T and Hambly, David M and Gross, Michael L and Cistola, David P and Goldman, William E
Biochemistry, ISSN 0006-2960, 04/2008, Volume 47, Issue 15, pp. 4427 - 4438
The virulence factor CBP is the most abundant protein secreted by Histoplasma capsulatum, a pathogenic fungus that causes histoplasmosis. Although the... 
CA2+-BINDING PROTEINS | C-13 | CHEMICAL-SHIFTS | CAPSULATUM | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR EXPERIMENTS | CONFORMATIONAL STABILITY | INTRACELLULAR PARASITISM | CALCIUM-DEPENDENCE | C-13-LABELED PROTEINS | MASS-SPECTROMETRY | Calcium-Binding Proteins - chemistry | Calcium-Binding Proteins - metabolism | Fungal Proteins - chemistry | Amino Acid Sequence | Peptides - chemistry | Protein Structure, Secondary | Calcium - metabolism | Molecular Sequence Data | Ultracentrifugation | Virulence Factors - chemistry | Histoplasma - pathogenicity | Disulfides - chemistry | Protein Denaturation | Nuclear Magnetic Resonance, Biomolecular | Virulence Factors - metabolism | Circular Dichroism | Dimerization | Fungal Proteins - metabolism | Histoplasma capsulatum | Genetic aspects | Chemical properties | Virulence (Microbiology) | Research | Calcium-binding proteins | Structure
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20. Full Text Determinants of cooperativity and site selectivity in human heal ileal bile acid binding protein
by Toke, Orsolya and Monsey, John D and DeKoster, Gregory T and Tochtrop, Gregroy P and Changguo Tang and Cistola, David P
Biochemistry, ISSN 0006-2960, 01/2006, Volume 45, Issue 3, p. 727
Enthalpy | Research | Binding proteins | Bile
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