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Protein-Carbohydrate Interactions

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Cover of 'Protein-Carbohydrate Interactions'

Table of Contents

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    Book Overview
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    Chapter 1 A Low-Volume, Parallel Copper-Bicinchoninic Acid (BCA) Assay for Glycoside Hydrolases
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    Chapter 2 Quantitative Kinetic Characterization of Glycoside Hydrolases Using High-Performance Anion-Exchange Chromatography (HPAEC)
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    Chapter 3 Measuring Enzyme Kinetics of Glycoside Hydrolases Using the 3,5-Dinitrosalicylic Acid Assay
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    Chapter 4 An Improved Kinetic Assay for the Characterization of Metal-Dependent Pectate Lyases
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    Chapter 5 Colorimetric Detection of Acetyl Xylan Esterase Activities
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    Chapter 6 Methods for Determining Glycosyltransferase Kinetics
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    Chapter 7 Analyzing Activities of Lytic Polysaccharide Monooxygenases by Liquid Chromatography and Mass Spectrometry
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    Chapter 8 Carbohydrate Depolymerization by Intricate Cellulosomal Systems
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    Chapter 9 Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions
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    Chapter 10 Quantifying CBM Carbohydrate Interactions Using Microscale Thermophoresis
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    Chapter 11 Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy
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    Chapter 12 Measuring the Biomechanical Loosening Action of Bacterial Expansins on Paper and Plant Cell Walls
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    Chapter 13 Bioinspired Assemblies of Plant Cell Walls for Measuring Protein-Carbohydrate Interactions by FRAP
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    Chapter 14 CBMs as Probes to Explore Plant Cell Wall Heterogeneity Using Immunocytochemistry
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    Chapter 15 Determining the Localization of Carbohydrate Active Enzymes Within Gram-Negative Bacteria
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    Chapter 16 Analysis of Complex Carbohydrate Composition in Plant Cell Wall Using Fourier Transformed Mid-Infrared Spectroscopy (FT-IR)
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    Chapter 17 Separation and Visualization of Glycans by Fluorophore-Assisted Carbohydrate Electrophoresis
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    Chapter 18 A Rapid Procedure for the Purification of 8-Aminopyrene Trisulfonate (APTS)-Labeled Glycans for Capillary Electrophoresis (CE)-Based Enzyme Assays
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    Chapter 19 Probing the Complex Architecture of Multimodular Carbohydrate-Active Enzymes Using a Combination of Small Angle X-Ray Scattering and X-Ray Crystallography
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    Chapter 20 Metagenomics and CAZyme Discovery
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    Chapter 21 Identification of Genes Involved in the Degradation of Lignocellulose Using Comparative Transcriptomics
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    Chapter 22 Isolation and Preparation of Extracellular Proteins from Lignocellulose Degrading Fungi for Comparative Proteomic Studies Using Mass Spectrometry
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    Chapter 23 Erratum to: Colorimetric Detection of Acetyl Xylan Esterase Activities
Attention for Chapter 22: Isolation and Preparation of Extracellular Proteins from Lignocellulose Degrading Fungi for Comparative Proteomic Studies Using Mass Spectrometry
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Chapter title
Isolation and Preparation of Extracellular Proteins from Lignocellulose Degrading Fungi for Comparative Proteomic Studies Using Mass Spectrometry
Chapter number 22
Book title
Protein-Carbohydrate Interactions
Published in
Methods in molecular biology, April 2017
DOI 10.1007/978-1-4939-6899-2_22
Pubmed ID
Book ISBNs
978-1-4939-6898-5, 978-1-4939-6899-2
Authors

Gruninger, Robert J., Tsang, Adrian, McAllister, Tim A., Robert J. Gruninger, Adrian Tsang, Tim A. McAllister

Editors

D. Wade Abbott, Alicia Lammerts van Bueren

Abstract

Fungi utilize a unique mechanism of nutrient acquisition involving extracellular digestion. To understand the biology of these microbes, it is important to identify and characterize the function of proteins that are secreted and involved in this process. Mass spectrometry-based proteomics is a powerful tool to study complex mixtures of proteins and understand how the proteins produced by an organism change in response to different conditions. Many fungi are efficient decomposers of plant cell wall, and anaerobic fungi are well recognized for their ability to digest lignocellulose. Here, we outline a protocol for the enrichment and isolation of proteins secreted by anaerobic fungi after growth on simple (glucose) and complex (straw and alfalfa hay) carbon sources. We provide detailed instruction on generating protein fragments and preparing these for proteomic analysis using reversed phase chromatography and mass spectrometry.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 8 100%

Demographic breakdown

Readers by professional status Count As %
Student > Doctoral Student 1 13%
Professor 1 13%
Student > Master 1 13%
Researcher 1 13%
Professor > Associate Professor 1 13%
Other 0 0%
Unknown 3 38%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 25%
Veterinary Science and Veterinary Medicine 1 13%
Immunology and Microbiology 1 13%
Unknown 4 50%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 22 April 2017.
All research outputs
#18,961,244
of 23,498,099 outputs
Outputs from Methods in molecular biology
#8,165
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Outputs of similar age
#237,222
of 311,489 outputs
Outputs of similar age from Methods in molecular biology
#159
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So far Altmetric has tracked 13,368 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 23rd percentile – i.e., 23% of its peers scored the same or lower than it.
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