A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids.

A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids.

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http://www.wikidata.org/entity/Q36785218
Position effect of cross-strand side-chain interactions on beta-hairpin formation.Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles.Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides.An α-helical core encodes the dual functions of the chlamydial protein IncA.Prediction of polyelectrolyte polypeptide structures using Monte Carlo conformational search methods with implicit solvation modeling.The turn sequence directs beta-strand alignment in designed beta-hairpins.De novo design of a monomeric three-stranded antiparallel beta-sheet.Ferredoxin and ferredoxin-heme maquettes.Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales.Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein.Structural characterization of NRAS isoform 5Solution assembly of a soluble, heteromeric, high affinity interleukin-2 receptor complex.Intrinsic α-helical and β-sheet conformational preferences: a computational case study of alanine.Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions.Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper.Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils.Trifluoroethanol induces the self-association of specific amphipathic peptides
P2860

A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids.

Item
http://www.wikidata.org/entity/Q36785218
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
A single-stranded amphipathic ...... l propensities of amino acids.
@en
type
label
A single-stranded amphipathic ...... l propensities of amino acids.
@en
prefLabel
A single-stranded amphipathic ...... l propensities of amino acids.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
A single-stranded amphipathic ...... l propensities of amino acids.
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P5875
P698