Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex.
about
Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitorModeling protein association mechanisms and kineticsElectrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.Systematic study of the substituted active C-terminus of hirudin.Free energy landscapes of encounter complexes in protein-protein associationKinetics of desolvation-mediated protein-protein binding.Structural basis of RGD-hirudin binding to thrombin: Tyr3 and five C-terminal residues are crucial for inhibiting thrombin activity.Thermodynamic and kinetic characterization of the protein Z-dependent protease inhibitor (ZPI)-protein Z interaction reveals an unexpected role for ZPI Lys-239.Automated prediction of protein association rate constants.Poisson-Boltzmann calculations of nonspecific salt effects on protein-protein binding free energies.Quantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP.Role of a conserved salt bridge between the PAS core and the N-terminal domain in the activation of the photoreceptor photoactive yellow proteinRate constants and mechanisms of intrinsically disordered proteins binding to structured targetsNMR solution structure of a novel hirudin variant HM2, N-terminal 1-47 and N64-->V + G mutant.Atomistic simulations of competition between substrates binding to an enzyme.Intrinsic disorder: signaling via highly specific but short-lived association.Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibitionA biosensor study indicating that entropy, electrostatics, and receptor glycosylation drive the binding interaction between interleukin-7 and its receptor.Electrostatic interactions in the association of proteins: an analysis of the thrombin-hirudin complex.Contribution of interactions with the core domain of hirudin to the stability of its complex with thrombin.Simulation of the diffusional association of barnase and barstar.The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast.Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms.Ionic interactions in the formation of the thrombin-hirudin complex.Enhancement of protein-protein association rate by interaction potential: accuracy of prediction based on local Boltzmann factor.Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.Ribosome surface properties may impose limits on the nature of the cytoplasmic proteome.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Probing the folding pathway of a consensus serpin using single tryptophan mutants.Treating ion distribution with Gaussian-based smooth dielectric function in DelPhi.On the protein-protein diffusional encounter complex.
P2860
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P2860
Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@en
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@nl
type
label
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@en
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@nl
prefLabel
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@en
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@nl
P2093
P356
P1433
P1476
Quantitative evaluation of the ...... the thrombin-hirudin complex.
@en
P2093
P304
P356
10.1021/BI00443A012
P407
P577
1989-08-01T00:00:00Z