Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer - Wikidata - wikimedia - TriplyDB

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

http://www.wikidata.org/entity/Q27658694

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Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as Metalloproteins Comparison of solution and crystal properties of Co(II)–substituted human carbonic anhydrase II Kinetic and crystallographic studies of the role of tyrosine 7 in the active site of human carbonic anhydrase II Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography Neutron Structure of Human Carbonic Anhydrase II: A Hydrogen-Bonded Water Network “Switch” Is Observed between pH 7.8 and 10.0 Rapid visualization of hydrogen positions in protein neutron crystallographic structures Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.NMR studies of active-site properties of human carbonic anhydrase II by using (15) N-labeled 4-methylimidazole as a local probe and histidine hydrogen-bond correlations.Neutron structure of human carbonic anhydrase II in complex with methazolamide: mapping the solvent and hydrogen-bonding patterns of an effective clinical drug.Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins Intrinsic proton-donating power of zinc-bound water in a carbonic anhydrase active site model estimated by NMR.Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.Joint X-ray and neutron refinement with phenix.refine.Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).Preliminary joint neutron time-of-flight and X-ray crystallographic study of human ABO(H) blood group A glycosyltransferase.Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum.Time-of-flight neutron diffraction study of bovine γ-chymotrypsin at the Protein Crystallography Station.Role of Trp19 and Tyr200 in catalysis by the γ-class carbonic anhydrase from Methanosarcina thermophila.Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase.Fifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography.Seeing the chemistry in biology with neutron crystallography.Carbonic anhydrases and their biotechnological applications.Neutron scattering techniques and applications in structural biology.Structure-Activity Relationships of Benzenesulfonamide-Based Inhibitors towards Carbonic Anhydrase Isoform Specificity.Mycolyltransferase from Mycobacterium tuberculosis in covalent complex with tetrahydrolipstatin provides insights into Antigen 85 catalysis.Exploring new strategies for cellulosic biofuels production Crystallography and Its Impact on Carbonic Anhydrase Research Is it the shape of the cavity, or the shape of the water in the cavity?

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P2860

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

http://www.wikidata.org/entity/Q27658694

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2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

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Neutron structure of human carbonic anhydrase II: implications for proton transfer

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David N Silverman

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John F Domsic

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Marat Mustyakimov

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Robert McKenna

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S Zoë Fisher

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P2860

A short history of SHELX

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin

The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer

Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism

Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II

Hydrogen Location in Stages of an Enzyme-Catalyzed Reaction: Time-of-Flight Neutron Structure of d -Xylose Isomerase with Bound d -Xylulose † ‡

Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II

Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement

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415-421

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scholarly article

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4651783

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10.1021/BI901995N

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3

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49

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Andrey Kovalevsky

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2010-01-01T00:00:00Z

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40755775

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20025241

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2893723

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