Analysis of proton chemical shifts in regular secondary structure of proteins.
about
Characterization of protein secondary structure from NMR chemical shiftsPREDITOR: a web server for predicting protein torsion angle restraintsElectronic properties of amino acid side chains: quantum mechanics calculation of substituent effects.BetaCore, a designed water soluble four-stranded antiparallel β-sheet proteinElongation of the BH8 beta-hairpin peptide: Electrostatic interactions in beta-hairpin formation and stabilityRelationship between chemical shift value and accessible surface area for all amino acid atoms.Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure.Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.Structure-oriented methods for protein NMR data analysisChemical shift tensor - the heart of NMR: Insights into biological aspects of proteinsNightShift: NMR shift inference by general hybrid model training--a framework for NMR chemical shift prediction.Predicting the redox state and secondary structure of cysteine residues using multi-dimensional classification analysis of NMR chemical shifts.Molecular modeling of the RNA binding N-terminal part of cowpea chlorotic mottle virus coat protein in solution with phosphate ions.Structure of ring-shaped Aβ₄₂ oligomers determined by conformational selection.CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shiftsConformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein.Empirical parameterization of a model for predicting peptide helix/coil equilibrium populations.Cation-pi interaction in a folded polypeptide.Type I and II β-turns prediction using NMR chemical shifts.Local protein backbone folds determined by calculated NMR chemical shifts.Design of supramolecular amino acids to template peptide folding.Insights into the molecular flexibility of θ-defensins by NMR relaxation analysis.Empirical isotropic chemical shift surfaces.Conformation of the Ras-binding domain of Raf studied by molecular dynamics and free energy simulations.Conformational distributions of denatured and unstructured proteins are similar to those of 20 × 20 blocked dipeptides.
P2860
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P2860
Analysis of proton chemical shifts in regular secondary structure of proteins.
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Analysis of proton chemical shifts in regular secondary structure of proteins.
@ast
Analysis of proton chemical shifts in regular secondary structure of proteins.
@en
Analysis of proton chemical shifts in regular secondary structure of proteins.
@nl
type
label
Analysis of proton chemical shifts in regular secondary structure of proteins.
@ast
Analysis of proton chemical shifts in regular secondary structure of proteins.
@en
Analysis of proton chemical shifts in regular secondary structure of proteins.
@nl
prefLabel
Analysis of proton chemical shifts in regular secondary structure of proteins.
@ast
Analysis of proton chemical shifts in regular secondary structure of proteins.
@en
Analysis of proton chemical shifts in regular secondary structure of proteins.
@nl
P356
P1476
Analysis of proton chemical shifts in regular secondary structure of proteins.
@en
P2093
P2888
P304
P356
10.1007/BF00175249
P577
1994-03-01T00:00:00Z