Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable
about
Accuracy of structure-derived properties in simple comparative models of protein structuresOsmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent statesCrystal structural analysis of protein-protein interactions drastically destabilized by a single mutationLong-range intra-protein communication can be transmitted by correlated side-chain fluctuations aloneCSI 2.0: a significantly improved version of the Chemical Shift Index.Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.Changes in protein structure at the interface accompanying complex formation.Advances in automated NMR protein structure determination.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarA novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.Sequence-structure mapping errors in the PDB: OB-fold domains.Optimization of binding electrostatics: charge complementarity in the barnase-barstar protein complex.DelPhi Web Server: A comprehensive online suite for electrostatic calculations of biological macromolecules and their complexes.A new scoring function for protein-protein docking that identifies native structures with unprecedented accuracy.Analysis on long-range residue-residue communication using molecular dynamics.Highly Efficient Computation of the Basal kon using Direct Simulation of Protein-Protein Association with Flexible Molecular Models.Simulations of the protein folding process using topology-based models depend on the experimental structure.Spin label method reveals barnase-barstar interaction: a temperature and viscosity dependence approach.SnapDock-template-based docking by Geometric Hashing.
P2860
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P2860
Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Discrepancies between the NMR ...... termined by NMR are unreliable
@ast
Discrepancies between the NMR ...... termined by NMR are unreliable
@en
Discrepancies between the NMR ...... termined by NMR are unreliable
@nl
type
label
Discrepancies between the NMR ...... termined by NMR are unreliable
@ast
Discrepancies between the NMR ...... termined by NMR are unreliable
@en
Discrepancies between the NMR ...... termined by NMR are unreliable
@nl
prefLabel
Discrepancies between the NMR ...... termined by NMR are unreliable
@ast
Discrepancies between the NMR ...... termined by NMR are unreliable
@en
Discrepancies between the NMR ...... termined by NMR are unreliable
@nl
P2093
P356
P1433
P1476
Discrepancies between the NMR ...... termined by NMR are unreliable
@en
P2093
G S Ratnaparkhi
J B Udgaonkar
R Varadarajan
S Ramachandran
P304
P356
10.1021/BI972857N
P407
P577
1998-05-12T00:00:00Z