The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein - Wikidata - awgldk - TriplyDB

The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein

The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein

http://www.wikidata.org/entity/Q34388738

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Structural and mechanistic fundamentals for designing of cellulases Structural, Biochemical, and Computational Characterization of the Glycoside Hydrolase Family 7 Cellobiohydrolase of the Tree-killing Fungus Heterobasidion irregulare O-glycosylation effects on family 1 carbohydrate-binding module solution structures Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module Product binding varies dramatically between processive and nonprocessive cellulase enzymes.Probing carbohydrate product expulsion from a processive cellulase with multiple absolute binding free energy methods.Modeling the self-assembly of the cellulosome enzyme complex.Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose Crystallization and preliminary X-ray diffraction analysis of Hypocrea jecorina Cel7A in two new crystal forms Asn124 of Cel5A from Hypocrea jecorina not only provides the N-glycosylation site but is also essential in maintaining enzymatic activity Cellulase linkers are optimized based on domain type and function: insights from sequence analysis, biophysical measurements, and molecular simulation.Cellulases from thermophilic fungi: recent insights and biotechnological potential.Computational investigation of glycosylation effects on a family 1 carbohydrate-binding module.Binding preferences, surface attachment, diffusivity, and orientation of a family 1 carbohydrate-binding module on cellulose.Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity.Computational investigation of the pH dependence of loop flexibility and catalytic function in glycoside hydrolases.Tick receptor for outer surface protein A from Ixodes ricinus - the first intrinsically disordered protein involved in vector-microbe recognition.Effects of the linker region on the structure and function of modular GH5 cellulases.Biochemical and Structural Characterizations of Two Dictyostelium Cellobiohydrolases from the Amoebozoa Kingdom Reveal a High Level of Conservation between Distant Phylogenetic Trees of Life.Analysis of the role of O-glycosylation in GH51 α-L-arabinofuranosidase from Pleurotus ostreatus Binding of cellulose binding modules reveal differences between cellulose substrates.Conformational flexibility of N-glycans in solution studied by REMD simulations.Effect of Linker Flexibility on the Catalytic Features of a Glycoside Hydrolase Family 45 Endoglucanase from Rhizopus stolonifer.Linker length and flexibility induces new cellobiohydrolase activity of PoCel6A from Penicillium oxalicum.Influence of Linker Length Variations on the Biomass-Degrading Performance of Heat-Active Enzyme Chimeras.A Dictyostelium cellobiohydrolase orthologue that affects developmental timing.The C-terminal region of xylanase domain in Xyn11A from Paenibacillus curdlanolyticus B-6 plays an important role in structural stability.A single-molecule analysis reveals morphological targets for cellulase synergy.A novel, highly efficient β-glucosidase with a cellulose-binding domain: characterization and properties of native and recombinant proteins.Distinct roles of N- and O-glycans in cellulase activity and stability.The influence of different linker modifications on the catalytic activity and cellulose affinity of cellobiohydrolase Cel7A from Hypocrea jecorina.Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum.Engineering enhanced cellobiohydrolase activity.The impact of O-glycan chemistry on the stability of intrinsically disordered proteins.Trichoderma reesei, a superior cellulase source for industrial applications Effect of Gum arabic on distribution behavior of nanocellulose fillers in starch film

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P2860

The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein

http://www.wikidata.org/entity/Q34388738

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2010 nî lūn-bûn

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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年论文

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Biophysical Journal

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Courtney B Taylor

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Gregg T Beckham

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Jakob Wohlert

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James F Matthews

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John M Yarbrough

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Lintao Bu

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Malin Bergenstråhle

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Michael F Crowley

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Michael G Resch

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P2860

Intrinsically unstructured proteins and their functions

Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

CHARMM: the biomolecular simulation program

A simple method for displaying the hydropathic character of a protein

Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D

Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus

Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing

The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei

Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei

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Michael E Himmel

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