The Alacoil: a very tight, antiparallel coiled-coil of helices.
about
Kinase activation through dimerization by human SH2-BDoing molecular biophysics: finding, naming, and picturing signal within complexityEvolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptorsAlanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant GAGA-factors in the nucleus and nucleolusRetrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteinsDeciphering the design of the tropomyosin moleculeAn alanine-zipper structure determined by long range intermolecular interactionsThe structure of BtuB with bound colicin E3 R-domain implies a transloconStructural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-TCrystal structure of a self-assembling lipopeptide detergent at 1.20 A.The Structure of a Soluble Chemoreceptor Suggests a Mechanism for Propagating Conformational Signals † ‡Predicting helix orientation for coiled-coil dimersThe membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.Probing designability via a generalized model of helical bundle geometryNMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.Investigating and Engineering Enzymes by Genetic Selection.Helix-packing motifs in membrane proteins.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 substitutionHuman immunodeficiency virus type 1 envelope glycoprotein oligomerization requires the gp41 amphipathic alpha-helical/leucine zipper-like sequenceHuman immunodeficiency virus type 1 and 2 envelope glycoproteins oligomerize through conserved sequencesMutations as trapdoors to two competing native conformations of the Rop-dimerBreaking symmetry in protein dimers: designs and functions.Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain.On the failure of de novo-designed peptides as biocatalysts.Structural Stability and Binding Strength of a Designed Peptide-Carbon Nanotube HybridStructures and ice-binding faces of the alanine-rich type I antifreeze proteins.Association of polyalanine and polyglutamine coiled coils mediates expansion disease-related protein aggregation and dysfunctionThe Structure and Topology of α-Helical Coiled Coils.Computational analysis of residue contributions to coiled-coil topology.How sequence directs bending in tropomyosin and other two-stranded alpha-helical coiled coils.Characterization of long and stable de novo single alpha-helix domains provides novel insight into their stability.Protein design and folding: template trapping of self-assembled helical bundles.De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures.Refolding studies on the tetrameric loop deletion mutant RM6 of ROP protein.
P2860
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P2860
The Alacoil: a very tight, antiparallel coiled-coil of helices.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@ast
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@en
type
label
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@ast
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@en
prefLabel
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@ast
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@en
P2093
P2860
P356
P1433
P1476
The Alacoil: a very tight, antiparallel coiled-coil of helices.
@en
P2093
D C Richardson
J S Richardson
K M Gernert
M C Surles
T H Labean
P2860
P304
P356
10.1002/PRO.5560041102
P577
1995-11-01T00:00:00Z