Structure of alpha-chymotrypsin refined at 1.68 A resolution
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The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsinMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesStructural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor DStructure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationshipsStructure of Human Prostasin, a Target for the Regulation of HypertensionExploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTERThe refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segmentX-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitorCrystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sitesAttempts to convert chymotrypsin to trypsinThe crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme).Conformational changes of alpha-chymotrypsin in a fibrillation-promoting condition: a molecular dynamics study.Probing immobilization mechanism of alpha-chymotrypsin onto carbon nanotube in organic media by molecular dynamics simulation.Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.The effects of reactive site location on the inhibitory properties of the serpin alpha(1)-antichymotrypsin.Crystallization, data collection and processing of the chymotrypsin-BTCI-trypsin ternary complexCharacterizing structural features of cuticle-degrading proteases from fungi by molecular modeling.Functionalized carbon nanotubes specifically bind to alpha-chymotrypsin's catalytic site and regulate its enzymatic function.High-precision measurement of hydrogen bond lengths in proteins by nuclear magnetic resonance methods.A Perspective on Reagent Diversity and Non-covalent Binding of Reactive Carbonyl Species (RCS) and Effector Reagents in Non-enzymatic Glycation (NEG): Mechanistic Considerations and Implications for Future Research.Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide.Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.Thermal and pH stability of "beta-benzyme".Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.Structure-based inhibitor design by using protein models for the development of antiparasitic agents.Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.Beauty is skin deep: a surface monolayer perspective on nanoparticle interactions with cells and bio-macromolecules.Design of peptide enzymes (pepzymes): surface-simulation synthetic peptides that mimic the chymotrypsin and trypsin active sites exhibit the activity and specificity of the respective enzyme.Using the Power of Organic Synthesis for Engineering the Interactions of Nanoparticles with Biological Systems.Solvent dielectric effects on protein dynamicsEnzymatic activity and thermal stability of PEG-alpha-chymotrypsin conjugates.Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site.Molecular mechanical properties of short-sequence peptide enzyme mimics.The processing of eIF4GI by human rhinovirus type 2 2A(pro): relationship to self-cleavage and role of zinc.Interaction of digestive enzymes with tunable light emitting quantum dots: a thorough Spectroscopic investigation.Systematic evaluation of bundled SPC water for biomolecular simulations.Structural and mechanistic basis of Parl activity and regulation.Significance of structural changes in proteins: expected errors in refined protein structures.Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building
P2860
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P2860
Structure of alpha-chymotrypsin refined at 1.68 A resolution
description
1985 nî lūn-bûn
@nan
1985 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
name
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@ast
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@en
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@nl
type
label
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@ast
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@en
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@nl
prefLabel
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@ast
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@en
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@nl
P1476
Structure of alpha-chymotrypsin refined at 1.68 A resolution
@en
P2093
P304
P356
10.1016/0022-2836(85)90314-6
P407
P577
1985-08-20T00:00:00Z