The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
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MSDmotif: exploring protein sites and motifsAtomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensisInhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexesX-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolutionThe crystal structure of a novel, inactive, lysine 49 PLA2 from Agkistrodon acutus venom: an ultrahigh resolution, AB initio structure determinationStructure determination and analysis of a bacterial chymotrypsin fromCellulomonas bogoriensisA previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding.Ultrahigh (0.93Å) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: Implications for the catalytic mechanismStructural Insight into Serine Protease Rv3671c that Protects M. tuberculosis from Oxidative and Acidic StressThe catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease actionProtonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completenessAtomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion holeNeutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.Challenging a paradigm: theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain.High-precision measurement of hydrogen bond lengths in proteins by nuclear magnetic resonance methods.Enumerating pathways of proton abstraction based on a spatial and electrostatic analysis of residues in the catalytic site.Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution.Distant homology modeling of LCAT and its validation through in silico targeting and in vitro and in vivo assaysTransient intermediates in enzymology, 1964-2008.How round is a protein? Exploring protein structures for globularity using conformal mapping.Hydrogen atoms in proteins: positions and dynamics.Ligand-Induced Proton Transfer and Low-Barrier Hydrogen Bond Revealed by X-ray Crystallography.Crystallization and preliminary X-ray crystallographic studies of a psychrophilic subtilisin-like protease Apa1 from Antarctic Pseudoalteromonas sp. strain AS-11Structure and protective efficacy of the Staphylococcus aureus autocleaving protease EpiP.Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin.A novel approach to the site-selective dual labelling of a protein via chemoselective cysteine modification.Protonate3D: assignment of ionization states and hydrogen coordinates to macromolecular structures.Polarizable atomic multipole X-ray refinement: application to peptide crystalsAtomic resolution structure of serine protease proteinase K at ambient temperature.Open and closed states of Candida antarctica lipase B: protonation and the mechanism of interfacial activation.The charge density distribution in a model compound of the catalytic triad in serine proteases.NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I.Selective protein degradation by ligand-targeted enzymes: towards the creation of catalytic antagonists.Observation of a short, strong hydrogen bond in the active site of hydroxynitrile lyase from Hevea brasiliensis explains a large pKa shift of the catalytic base induced by the reaction intermediate.The influence of solvation on short strong hydrogen bonds: a density functional theory study of the Asp-His interaction in subtilisins.Precise Probing of Residue Roles by Post-Translational β,γ-C,N Aza-Michael Mutagenesis in Enzyme Active Sites.Connecting Classical QSAR and LERE Analyses Using Modern Molecular Calculations, LERE-QSAR (VI): Hydrolysis of Substituted Hippuric Acid Phenyl Esters by Trypsin.In vitro Ca(2+)-dependent maturation of milk-clotting recombinant Epr: minor extracellular protease: from Bacillus licheniformis.
P2860
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P2860
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@ast
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@en
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@nl
type
label
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@ast
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@en
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@nl
prefLabel
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@ast
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@en
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@nl
P2093
P356
P1433
P1476
The 0.78 A structure of a serine protease: Bacillus lentus subtilisin
@en
P2093
P304
13446-13452
P356
10.1021/BI9813983
P407
P577
1998-09-01T00:00:00Z