Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data
about
KinImmerse: Macromolecular VR for NMR ensemblesNMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognitionLanthanide binding and IgG affinity construct: Potential applications in solution NMR, MRI, and luminescence microscopyArtificial affinity proteins as ligands of immunoglobulinsA practical implicit solvent potential for NMR structure calculation.The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A.Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticityDesign of a modular protein-based MRI contrast agent for targeted application.Computational protein design with electrostatic focusing: experimental characterization of a conditionally folded helical domain with a reduced amino acid alphabet.Determination of protein backbone structures from residual dipolar couplings.Structure-based Design of Peptides with High Affinity and Specificity to HER2 Positive TumorsA Conjugate Based on Anti-HER2 Diaffibody and Auristatin E Targets HER2-Positive Cancer Cells.Interdomain orientation of cardiac troponin C characterized by paramagnetic relaxation enhancement NMR reveals a compact stateAn encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteinsDetecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping.A genetically encoded boronate-containing amino acid.Folding processes of the B domain of protein A to the native state observed in all-atom ab initio folding simulations.Engineered solubility tag for solution NMR of proteins.3-2-1: Structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix.Automatic C chemical shift reference correction for unassigned protein NMR spectra
P2860
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P2860
Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data
description
2004 nî lūn-bûn
@nan
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Validation of helical tilt ang ...... dipolar coupling and NOE data
@ast
Validation of helical tilt ang ...... dipolar coupling and NOE data
@en
Validation of helical tilt ang ...... dipolar coupling and NOE data
@nl
type
label
Validation of helical tilt ang ...... dipolar coupling and NOE data
@ast
Validation of helical tilt ang ...... dipolar coupling and NOE data
@en
Validation of helical tilt ang ...... dipolar coupling and NOE data
@nl
prefLabel
Validation of helical tilt ang ...... dipolar coupling and NOE data
@ast
Validation of helical tilt ang ...... dipolar coupling and NOE data
@en
Validation of helical tilt ang ...... dipolar coupling and NOE data
@nl
P2860
P356
P1433
P1476
Validation of helical tilt ang ...... dipolar coupling and NOE data
@en
P2093
James M Aramini
P2860
P304
P356
10.1110/PS.03351704
P577
2004-02-01T00:00:00Z