about
Local order in the unfolded state: conformational biases and nearest neighbor interactionsCrystal structure of group II intron domain 1 reveals a template for RNA assemblyA short linear peptide that folds into a native stable beta-hairpin in aqueous solutionExtremely rapid protein folding in the absence of intermediates.Predicting β-turns in protein using kernel logistic regressionFolding and stability of the three-stranded beta-sheet peptide Betanova: insights from molecular dynamics simulations.NMR characterization of partially folded and unfolded conformational ensembles of proteins.Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains.Proline-glutamate chimera's side chain conformation directs the type of β-hairpin structure.A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin.New theoretical methodology for elucidating the solution structure of peptides from NMR data. II. Free energy of dominant microstates of Leu-enkephalin and population-weighted average nuclear Overhauser effects intensities.Characterisation of the isolated Che Y C-terminal fragment (79-129)--Exploring the structure/stability/folding relationship of the alpha/beta parallel protein Che Y.Using synchrotron radiation-based infrared microspectroscopy to reveal microchemical structure characterization: frost damaged wheat vs. normal wheat.Conformational propensities and residual structures in unfolded peptides and proteins.Charge neutralization as the major factor for the assembly of nucleocapsid-like particles from C-terminal truncated hepatitis C virus core protein.What should the Z-score of native protein structures be?Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating asx and β-type like turn conformations.N-Terminal domain of HTLV-I integrase. Complexation and conformational studies of the zinc finger.Protein secondary structures (alpha-helix and beta-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach.Multicomponent peak modeling of protein secondary structures: comparison of gaussian with lorentzian analytical methods for plant feed and seed molecular biology and chemistry research.Molecular dynamics simulations of beta-hairpin folding.Effects of turn residues on beta-hairpin folding--a molecular dynamics study.Helix stability in barstar peptides.Elucidating the folding problem of helical peptides using empirical parameters.Interactions Responsible for the pH Dependence of the beta-Hairpin Conformational Population Formed by a Designed Linear PeptidePrediction of four kinds of simple supersecondary structures in protein by using chemical shifts
P2860
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P2860
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 1993
@uk
name
Peptide conformation and protein folding
@en
Peptide conformation and protein folding
@nl
type
label
Peptide conformation and protein folding
@en
Peptide conformation and protein folding
@nl
prefLabel
Peptide conformation and protein folding
@en
Peptide conformation and protein folding
@nl
P1476
Peptide conformation and protein folding
@en
P2093
H.Jane Dyson
Peter E. Wright
P356
10.1016/0959-440X(93)90203-W
P577
1993-02-01T00:00:00Z