Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.
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Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.Neutron structure of human carbonic anhydrase II in complex with methazolamide: mapping the solvent and hydrogen-bonding patterns of an effective clinical drug.Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenaseFifteen years of the Protein Crystallography Station: the coming of age of macromolecular neutron crystallography.Insights into the binding mode of sulphamates and sulphamides to hCA II: crystallographic studies and binding free energy calculations.Carbonic Anhydrases: Role in pH Control and Cancer.
P2860
Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.
description
2015 nî lūn-bûn
@nan
2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@ast
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@en
type
label
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@ast
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@en
prefLabel
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@ast
Joint neutron crystallographic ...... zyme-mediated proton transfer.
@en
P2093
P2860
P50
P356
P1476
Joint neutron crystallographic ...... nzyme-mediated proton transfer
@en
P2093
Andreas Ostermann
Clifford J Unkefer
Robert McKenna
Suzanne Zoë Fisher
P2860
P304
P356
10.1073/PNAS.1502255112
P407
P577
2015-04-20T00:00:00Z