A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
about
Invariant gly residue is important for α-defensin folding, dimerization, and function: a case study of the human neutrophil α-defensin HNP1A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroThe centriolar protein CPAP G-box: an amyloid fibril in a single domainStructure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein designFactors contributing to decreased protein stability when aspartic acid residues are in β-sheet regionsCrystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2Hydrophobic Surface Burial Is the Major Stability Determinant of a Flat, Single-layer β-Sheetβ-Strand Flipping and Slipping Triggered by Turn Replacement Reveal the Opportunistic Nature of β-Strand PairingComputer-Based Redesign of a β Sandwich Protein Suggests that Extensive Negative Design Is Not Required for De Novo β Sheet DesignARNT PAS-B has a fragile native state structure with an alternative -sheet register nearby in sequence spaceA transcriptional activating region with two contrasting modes of protein interaction.Protein stability: a crystallographer's perspectiveProtein design: Past, present, and futureElongation of the BH8 beta-hairpin peptide: Electrostatic interactions in beta-hairpin formation and stabilityA knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding.Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Evolution rescues folding of human immunodeficiency virus-1 envelope glycoprotein GP120 lacking a conserved disulfide bondThe identification of conserved interactions within the SH3 domain by alignment of sequences and structures.Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backboneThe geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.Quinary structure modulates protein stability in cells.Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a β-hairpin.Sequence periodicity and secondary structure propensity in model proteins.Synthetic protein design: construction of a four-stranded beta-sheet structure and evaluation of its integrity in methanol-water systems.Position effect of cross-strand side-chain interactions on beta-hairpin formation.Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformationParallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Exploring beta-sheet structure and interactions with chemical model systems.Mirrors in the PDB: left-handed alpha-turns guide design with D-amino acids.Statistical analysis and molecular dynamics simulations of ambivalent α-helices.In vivo protein stabilization based on fragment complementation and a split GFP system.Quantifying amino acid conformational preferences and side-chain-side-chain interactions in beta-hairpins.Role of backbone solvation in determining thermodynamic beta propensities of the amino acids.Residue level quantification of protein stability in living cells.Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides.A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scalesReconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids.A statistical analysis of the PPII propensity of amino acid guests in proline-rich peptides.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.
P2860
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P2860
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@en
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@nl
type
label
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@en
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@nl
prefLabel
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@en
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@nl
P2093
P356
P1433
P1476
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
@en
P2093
P304
P356
10.1021/BI00184A020
P407
P577
1994-05-01T00:00:00Z