Investigation of the backbone dynamics of the IgG-binding domain of streptococcal protein G by heteronuclear two-dimensional 1H-15N nuclear magnetic resonance spectroscopy.
about
Heparin binding by the HIV-1 tat protein transduction domainStructure and dynamics of de novo proteins from a designed superfamily of 4-helix bundlesOverall rotational diffusion and internal mobility in domain II of protein G from Streptococcus determined from 15N relaxation data.Residue level quantification of protein stability in living cells.Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes.Long dynamics simulations of proteins using atomistic force fields and a continuum representation of solvent effects: calculation of structural and dynamic properties.Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements.Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same foldThe de novo design of a rubredoxin-like Fe site.The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.Comparison of (13)C(alpha)H and (15)NH backbone dynamics in protein GB1.Probing the role of packing specificity in protein design.Soluble mimics of a chemokine receptor: chemokine binding by receptor elements juxtaposed on a soluble scaffoldCore mutants of the immunoglobulin binding domain of streptococcal protein G: stability and structural integrity.A molecular dynamics simulation study of segment B1 of protein G.Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations.The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition.Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D ²H-¹³C-¹³C Solid-State NMR SpectroscopyUnraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.The consistency of large concerted motions in proteins in molecular dynamics simulations.Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae.Coupling backbone flexibility and amino acid sequence selection in protein design.Mechanics and dynamics of B1 domain of protein G: role of packing and surface hydrophobic residues.Determination of methyl 13C-15N dipolar couplings in peptides and proteins by three-dimensional and four-dimensional magic-angle spinning solid-state NMR spectroscopy.Protein molecular dynamics with the generalized born/ACE solvent model
P2860
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P2860
Investigation of the backbone dynamics of the IgG-binding domain of streptococcal protein G by heteronuclear two-dimensional 1H-15N nuclear magnetic resonance spectroscopy.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Investigation of the backbone ...... gnetic resonance spectroscopy.
@ast
Investigation of the backbone ...... gnetic resonance spectroscopy.
@en
type
label
Investigation of the backbone ...... gnetic resonance spectroscopy.
@ast
Investigation of the backbone ...... gnetic resonance spectroscopy.
@en
prefLabel
Investigation of the backbone ...... gnetic resonance spectroscopy.
@ast
Investigation of the backbone ...... gnetic resonance spectroscopy.
@en
P2093
P2860
P356
P1433
P1476
Investigation of the backbone ...... gnetic resonance spectroscopy.
@en
P2093
Barchi JJ Jr
Grasberger B
Gronenborn AM
P2860
P356
10.1002/PRO.5560030103
P577
1994-01-01T00:00:00Z