Controlling topology and native-like behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils.
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De novo proteins from designed combinatorial librariesRetrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteinsAccommodation of a highly symmetric core within a symmetric protein superfoldStructural basis for the enhanced stability of highly fluorinated proteinsDe novo design of helical bundles as models for understanding protein folding and function.Recent advances in our understanding of protein conformational stability from a pharmaceutical perspective.Fluorinated Coiled-Coil Proteins Prepared In Vivo Display Enhanced Thermal and Chemical Stability This work was supported by a grant from the U.S. Army Research Office. Y. Tang is supported by a Whitaker Graduate Research Fellowship. We thank Dr. GaInvestigating and Engineering Enzymes by Genetic Selection.Rotational orientation of monomers within a designed homo-oligomer transmembrane helical bundle.Selection and structural analysis of de novo proteins from an alpha3beta3 genetic library.Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedronExploration of the structural features defining the conduction properties of a synthetic ion channel.Coiled coils at the edge of configurational heterogeneity. Structural analyses of parallel and antiparallel homotetrameric coiled coils reveal configurational sensitivity to a single solvent-exposed amino acid substitutionProbing the role of packing specificity in protein design.Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain.Synthetic, biologically active amphiphilic peptidesα-Helical coiled-coil peptide materials for biomedical applications.Computational analysis of residue contributions to coiled-coil topology.Engineering of betabellin-15D: a 64 residue beta sheet protein that forms long narrow multimeric fibrils.De Novo Construction of Redox Active Proteins.Automated design of the surface positions of protein helicesCoupling backbone flexibility and amino acid sequence selection in protein design.Noncovalent binding of a reaction intermediate by a designed helix-loop-helix motif-implications for catalyst design.Inhibition of amyloid aggregation by formation of helical assemblies.
P2860
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P2860
Controlling topology and native-like behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Controlling topology and nativ ...... el four-stranded coiled coils.
@ast
Controlling topology and nativ ...... el four-stranded coiled coils.
@en
type
label
Controlling topology and nativ ...... el four-stranded coiled coils.
@ast
Controlling topology and nativ ...... el four-stranded coiled coils.
@en
prefLabel
Controlling topology and nativ ...... el four-stranded coiled coils.
@ast
Controlling topology and nativ ...... el four-stranded coiled coils.
@en
P356
P1433
P1476
Controlling topology and nativ ...... el four-stranded coiled coils.
@en
P2093
P304
P356
10.1021/BI960095A
P407
P577
1996-05-01T00:00:00Z