The spectrin repeat folds into a three-helix bundle in solution.
about
Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitroA new twist to coiled coilSolution structural studies on human erythrocyte alpha-spectrin tetramerization siteThe Structure of the Plakin Domain of Plectin Reveals a Non-canonical SH3 Domain Interacting with Its Fourth Spectrin RepeatProbing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochlorideMultiCoil: a program for predicting two- and three-stranded coiled coilsThe folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Identification of the main ubiquitination site in human erythroid alpha-spectrin.Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin.Expression profiling reveals novel hypoxic biomarkers in peripheral blood of adult mice exposed to chronic hypoxia.Complex folding kinetics of a multidomain protein.Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteinsApparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domainsSeparating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the alpha beta spectrin self-association binding site.Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanismsElectron Microscopy and Image Processing: Essential Tools for Structural Analysis of Macromolecules.Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.NMR assignments and relaxation studies of Thiobacillus versutus ferrocytochrome c-550 indicate the presence of a highly mobile 13-residues long C-terminal tail.Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.Stability of the dystrophin rod domain fold: evidence for nested repeating units.From coiled coils to small globular proteins: design of a native-like three-helix bundle.Folding intermediates of a model three-helix bundle protein. Pressure and cold denaturation studies.Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study.Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit.RACK1 (receptor for activated C-kinase 1) interactions with spectrin repeat elements.States and transitions during forced unfolding of a single spectrin repeat.
P2860
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P2860
The spectrin repeat folds into a three-helix bundle in solution.
description
1996 nî lūn-bûn
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1996年の論文
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年學術文章
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1996年學術文章
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name
The spectrin repeat folds into a three-helix bundle in solution.
@en
The spectrin repeat folds into a three-helix bundle in solution.
@nl
type
label
The spectrin repeat folds into a three-helix bundle in solution.
@en
The spectrin repeat folds into a three-helix bundle in solution.
@nl
prefLabel
The spectrin repeat folds into a three-helix bundle in solution.
@en
The spectrin repeat folds into a three-helix bundle in solution.
@nl
P2860
P50
P1433
P1476
The spectrin repeat folds into a three-helix bundle in solution
@en
P2093
P2860
P304
P356
10.1016/0014-5793(96)00251-7
P407
P577
1996-04-01T00:00:00Z