The Calpha ---H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions.
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Homology modeling of the cation binding sites of Na+K+-ATPase.Functional analysis of subunit e of the F1Fo-ATP synthase of the yeast Saccharomyces cerevisiae: importance of the N-terminal membrane anchor regionSolute-solvent complex switching dynamics of chloroform between acetone and dimethylsulfoxide-two-dimensional IR chemical exchange spectroscopyGenomic analysis of membrane protein families: abundance and conserved motifsCalpha-H...O = C hydrogen bonds contribute to the specificity of RGD cell-adhesion interactionsArchitecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin ZStructural organization and interactions of transmembrane domains in tetraspanin proteinsCarbon-oxygen hydrogen bonding in biological structure and functionTransmembrane helix dimerization: beyond the search for sequence motifsStructural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex.Structural and Functional Characterization of Nonstructural Protein 2 for Its Role in Hepatitis C Virus AssemblyStructural basis for a pH-sensitive calcium leak across membranesAn α/β-Peptide Helix Bundle with a Pure β 3 -Amino Acid Core and a Distinctive Quaternary StructureSubstitution of Ala for Tyr567 in RB69 DNA Polymerase Allows dAMP To Be Inserted opposite 7,8-Dihydro-8-oxoguanine,The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfaceInsights into Base Selectivity from the 1.8 Å Resolution Structure of an RB69 DNA Polymerase Ternary ComplexVariation in Mutation Rates Caused by RB69pol Fidelity Mutants Can Be Rationalized on the Basis of Their Kinetic Behavior and Crystal StructurespH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRDimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environmentsBinding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural StudyA screen for nigericin-resistant yeast mutants revealed genes controlling mitochondrial volume and mitochondrial cation homeostasis.Molecular dynamics simulation studies of GLUT4: substrate-free and substrate-induced dynamics and ATP-mediated glucose transport inhibitionGenome-wide analysis of major intrinsic proteins in the tree plant Populus trichocarpa: characterization of XIP subfamily of aquaporins from evolutionary perspectiveMPlot--a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteinsAnalysis of side-chain rotamers in transmembrane proteins.Comparison of helix interactions in membrane and soluble alpha-bundle proteins.NCI: A server to identify non-canonical interactions in protein structures.Membrane protein folding: beyond the two stage model.Solid state NMR: The essential technology for helical membrane protein structural characterization.Observation of glycine zipper and unanticipated occurrence of ambidextrous helices in the crystal structure of a chiral undecapeptideSequence-specific dimerization of a transmembrane helix in amphipol A8-35.Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers.The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.Understanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?Membrane Fusion and Infection of the Influenza Hemagglutinin.Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structureGlycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Naturally evolved G protein-coupled receptors adopt metastable conformations.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site.
P2860
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P2860
The Calpha ---H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@ast
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@en
type
label
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@ast
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@en
prefLabel
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@ast
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@en
P2093
P2860
P356
P1476
The Calpha ---H...O hydrogen b ...... nsmembrane helix interactions.
@en
P2093
Engelman DM
Ubarretxena-Belandia I
P2860
P304
P356
10.1073/PNAS.161280798
P407
P577
2001-07-01T00:00:00Z