Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality - Wikidata - wikimedia - TriplyDB

Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality

Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality

http://www.wikidata.org/entity/Q24605540

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Cryo-electron microscopy structure of the TRPV2 ion channel A Diiron Protein Autogenerates a Valine-Phenylalanine Cross-Link Symerythrin Structures at Atomic Resolution and the Origins of Rubrerythrins and the Ferritin-Like Superfamily In Human Pseudouridine Synthase 1 (hPus1), a C-Terminal Helical Insert Blocks tRNA from Binding in the Same Orientation as in the Pus1 Bacterial Homologue TruA, Consistent with Their Different Target Selectivities The structure of latherin, a surfactant allergen protein from horse sweat and saliva Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria Arabidopsis Accelerated Cell Death 11, ACD11, Is a Ceramide-1-Phosphate Transfer Protein and Intermediary Regulator of Phytoceramide Levels High-resolution crystal structure of the recombinant diheme cytochrome c from Shewanella baltica (OS155)Structural basis of the proinflammatory signaling complex mediated by TSLP FF12MC: A revised AMBER forcefield and new protein simulation protocol.The accommodation index measures the perturbation associated with insertions and deletions in coiled-coils: Application to understand signaling in histidine kinases.(φ,ψ)₂ motifs: a purely conformation-based fine-grained enumeration of protein parts at the two-residue level.Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold Fluctuations of an exposed π-helix involved in lipoxygenase substrate recognition A giant molecular proton pump: structure and mechanism of respiratory complex I.Structural and functional characterization of TesB from Yersinia pestis reveals a unique octameric arrangement of hotdog domains Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.An Accurate Model for Biomolecular Helices and Its Application to Helix Visualization.Peroxiredoxins in parasites.Structural and biophysical insight into cholesteryl ester-transfer protein.Impact of helix irregularities on sequence alignment and homology modeling of G protein-coupled receptors.The mechanism of coupling between electron transfer and proton translocation in respiratory complex I.Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Intramolecular backbone···backbone hydrogen bonds in polypeptide conformations. The other way around: ɛ-turn.An Extra Amino Acid Residue in Transmembrane Domain 10 of the γ-Aminobutyric Acid (GABA) Transporter GAT-1 Is Required for Efficient Ion-coupled Transport.Dissecting π-helices: sequence, structure and function.Function of the M1 π-helix in endplate receptor activation and desensitization.Structure of mammalian respiratory complex I The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases.The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs.Structure and antagonism of the receptor complex mediated by human TSLP in allergy and asthma.Dihedral-based segment identification and classification of biopolymers I: proteins A series of PDB-related databanks for everyday needs.Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function.Amino Acids in Nine Ligand-Prefer Ramachandran Regions Mollib: a molecular and NMR data analysis software.Geometry motivated alternative view on local protein backbone structures.Protein insertions and deletions enabled by neutral roaming in sequence space.N-alkylacylamides in thin films display infrared spectra of 3₁₀-, α-, and π-helices with visible static and dynamic growth phases.

P2860

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P2860

Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality

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2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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Evolutionary origin of a secon ...... enhance protein functionality

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J.JMB.2010.09.034

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Journal of Molecular Biology

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Evolutionary origin of a secon ...... enhance protein functionality

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Daniel J Arp

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Richard B Cooley

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In the light of directed evolution: pathways of adaptive protein evolution

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

The Protein Data Bank

The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease

The pi-helix translates structure into function

Structure of bacteriorhodopsin at 1.55 A resolution

Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution

Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA

Structural consequences of effector protein complex formation in a diiron hydroxylase

A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold

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protein structure

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