Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
about
Comparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.Computational de novo design of a four-helix bundle protein--DND_4HB.Amino acid alphabet reduction preserves fold information contained in contact interactions in proteins.Sequence periodicity and secondary structure propensity in model proteins.Comparative characterization of random-sequence proteins consisting of 5, 12, and 20 kinds of amino acids.De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growthBinding of small molecules to cavity forming mutants of a de novo designed protein.Directed evolution of the peroxidase activity of a de novo-designed protein.Design, expression, and purification of de novo transmembrane "hairpin" peptides.Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.An evolution-based approach to De Novo protein design and case study on Mycobacterium tuberculosis.Relative stability of de novo four-helix bundle proteins: insights from coarse grained molecular simulations.De Novo Proteins with Life-Sustaining Functions Are Structurally DynamicA de novo protein confers copper resistance in Escherichia coli.A protein constructed de novo enables cell growth by altering gene regulation.Folding helical proteins in explicit solvent using dihedral-biased tempering.Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins.Predicting protein dynamics from structural ensembles.Generic coarse-grained model for protein folding and aggregation.Hierarchical cascades of instability govern the mechanics of coiled coils: helix unfolding precedes coil unzipping.Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7.Intrinsically unstructured proteins by design-electrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer.Hierarchical design of artificial proteins and complexes toward synthetic structural biology.
P2860
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P2860
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@ast
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@en
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@nl
type
label
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@ast
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@en
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@nl
prefLabel
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@ast
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@en
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@nl
P2093
P2860
P356
P1433
P1476
Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles
@en
P2093
Abigail Go
Michael H Hecht
P2860
P304
P356
10.1110/PS.073377908
P577
2008-05-01T00:00:00Z