A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR data.
about
The solution structure of the Mg2+form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cellsSolution NMR Structures of Productive and Non-productive Complexes between the A and B Domains of the Cytoplasmic Subunit of the Mannose Transporter of the Escherichia coli Phosphotransferase SystemSolution Structure of the IIAChitobiose-IIBChitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemCombined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I DimerSolution Structure of the IIAChitobiose-HPr Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemUsing the experimentally determined components of the overall rotational diffusion tensor to restrain molecular shape and size in NMR structure determination of globular proteins and protein-protein complexes.Parameterization of solvent-protein interaction and its use on NMR protein structure determinationSimplified AIP-II Peptidomimetics Are Potent Inhibitors of Staphylococcus aureus AgrC Quorum Sensing Receptors.Characterization of structural elements in native autoinducing peptides and non-native analogues that permit the differential modulation of AgrC-type quorum sensing receptors in Staphylococcus aureus.Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxinAn FFT-based method for modeling protein folding and binding under crowding: benchmarking on ellipsoidal and all-atom crowdersStructural characterization of native autoinducing peptides and abiotic analogues reveals key features essential for activation and inhibition of an AgrC quorum sensing receptor in Staphylococcus aureus.An overview of tools for the validation of protein NMR structures.Xplor-NIH for Molecular Structure Determination from NMR and Other Data Sources.Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch.Theory and practice of using solvent paramagnetic relaxation enhancement to characterize protein conformational dynamics.
P2860
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P2860
A pseudopotential for improving the packing of ellipsoidal protein structures determined from NMR data.
description
2007 nî lūn-bûn
@nan
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
A pseudopotential for improvin ...... ures determined from NMR data.
@ast
A pseudopotential for improvin ...... ures determined from NMR data.
@en
type
label
A pseudopotential for improvin ...... ures determined from NMR data.
@ast
A pseudopotential for improvin ...... ures determined from NMR data.
@en
prefLabel
A pseudopotential for improvin ...... ures determined from NMR data.
@ast
A pseudopotential for improvin ...... ures determined from NMR data.
@en
P356
P1476
A pseudopotential for improvin ...... ures determined from NMR data.
@en
P2093
G Marius Clore
P304
P356
10.1021/JP076244O
P407
P577
2007-12-19T00:00:00Z