Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.
about
The structure of the ankyrin-binding site of -spectrin reveals how tandem spectrin-repeats generate unique ligand-binding propertiesProbing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochlorideStabilization of the spectrin-like domains of nesprin-1α by the evolutionarily conserved "adaptive" domain.Shapes of Red Blood Cells: Comparison of 3D Confocal Images with the Bilayer-Couple Model.Extending a spectrin repeat unit. II: rupture behaviorComplex folding kinetics of a multidomain protein.Spectrin domains lose cooperativity in forced unfolding.Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteinsThe folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domainsPathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding.Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.Thermal stabilities of brain spectrin and the constituent repeats of subunits.Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanismsHybrid spectrin type repeats produced by exon-skipping in dystrophin.Molecular epitopes of the ankyrin-spectrin interaction.Stability of dystrophin STR fragments in relation to junction helicity.Structural organization of the nine spectrin repeats of Kalirin.Conformational stabilities of the structural repeats of erythroid spectrin and their functional implications.
P2860
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P2860
Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.
description
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name
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@ast
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@en
type
label
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@ast
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@en
prefLabel
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@ast
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@en
P2860
P356
P1476
Stabilities of folding of clus ...... n erythroid spectrin tetramer.
@en
P2093
Julie A Cummings
Ruby I MacDonald
P2860
P304
P356
10.1073/PNAS.0308059100
P407
P577
2004-01-27T00:00:00Z