13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.
about
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.Assessing the Ability of Spectroscopic Methods to Determine the Difference in the Folding Propensities of Highly Similar β-Hairpins.
P2860
13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.
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13C structuring shifts for the ...... ross-strand H-bonded residues.
@en
13C structuring shifts for the ...... ross-strand H-bonded residues.
@nl
type
label
13C structuring shifts for the ...... ross-strand H-bonded residues.
@en
13C structuring shifts for the ...... ross-strand H-bonded residues.
@nl
prefLabel
13C structuring shifts for the ...... ross-strand H-bonded residues.
@en
13C structuring shifts for the ...... ross-strand H-bonded residues.
@nl
P2093
P2860
P1476
13C structuring shifts for the ...... ross-strand H-bonded residues.
@en
P2093
Brandon L Kier
James M Stewart
Michele Scian
Niels H Andersen
P2860
P2888
P304
P356
10.1007/S10858-013-9749-3
P577
2013-07-14T00:00:00Z