Peptide Self-Assembly -

Peptide Self-Assembly

Methods and Protocols
Buch | Hardcover
452 Seiten
2018 | 1st ed. 2018
Humana Press Inc. (Verlag)
978-1-4939-7809-0 (ISBN)
192,59 inkl. MwSt
This volume details methods and protocols on b-sheet assemblies and collagen. Divided into three parts chapters focus on expanding use of solid-state NMR as a powerful method to enhance structural understanding of self-assembled peptide materials, methods for the design, synthesis, and application of self-assembled peptide materials, and structural and mechanistic analyses of pathological amyloid systems that provide novel ways to assess function of the various possible aggregates as well to determine how the structure of these materials correlates to function/dysfunction in the biological context. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.

Authoritative and cutting-edge, Peptide Self-Assembly: Methods and Protocols aims to capture modern methods that span the breadth of the exciting and expanding field of peptide self-assembly.

Methods for Structural Analysis of Aggregates Formed by Self-Assembling Peptides.- Solid state NMR Structura.- Characterization of Self-assembled Peptides With Selective 13C and 15N Isotopic LabelsATR-FTIR Analysis of Amyloid Proteins.- Imaging Protein Fibers at the Nanoscale and In Situ.- Replica Exchange Molecular Dynamics: A Practical Application Protocol with Solutions to Common Problems and a Peptide Aggregation and Self-Assembly Example.- An Aggregate Weight-normalized thioflavin-T Measurement Scale For Characterizing Polymorphic Amyloids And Assembly Intermediates.- Nanoparticle Tracking for Protein Aggregation Research.- Peptide Self-assembly Measured using Fluorescence Correlation Spectroscopy.- A General Method to Prepare Peptide-based Supramolecular Hydrogels.- Recursive Directional Ligation Approach for Cloning Recombinant Spider Silks.- Synthesis of Mikto-Arm Star Peptide Conjugates.- Synthesis and Evaluation of Self—Assembled Nanostructures of Peptide—π chromophore conjugates.- Programmable Fabrication of Multi-layer Collagen Nanosheets of Defined Composition.- Practical Considerations in the Design and use of Immunologically Active Fibrillar Peptide Assemblies.- Microwave-assisted Synthesis and Immunological Evaluation of Self-Assembling Peptide Vaccines.- Preparation and Screening of Catalytic Amyloid Assemblies.-Self-assembly of Filamentous Cell Penetrating Peptides for Gene Delivery.- Biogelx: Cell Culture on Gels based on Aromatic Peptide Amphiphiles.- Production and use of Recombinant Aβ for Aggregation Studies.- Disaggregation of Ab42 for Structural and Biochemical Studies.- Preparation of Stable Amyloid-β Oligomers Without Perturbative Methods.- Discriminating Strains of Self-Propagating Protein Aggregates Using a Conformational Stability Assay.-  Model Phospholipid Liposomes to Study the b-Amyloid-Peptide-Induced Membrane Disruption.- Using Molecular Tweezers to Remodel Abnormal Protein Self-assembly and Inhibit the Toxicity of Amyloidogenic Proteins.- Incorporation of an azobenzene b-turn Peptidomimetic into Amyloid-b to Probe Potential Structural Motifs Leading to b-sheet self-assembly.- Solid State NMR Studies of Amyloid Materials: A Protocol to Define an Atomic Model of Aβ(1–42) in Amyloid Fibrils.- Experimental and Computational Protocols for Studies of Cross-seeding Amyloid Assemblies.

Erscheinungsdatum
Reihe/Serie Methods in Molecular Biology ; 1777
Zusatzinfo 53 Illustrations, color; 77 Illustrations, black and white; XV, 452 p. 130 illus., 53 illus. in color.
Verlagsort Totowa, NJ
Sprache englisch
Maße 178 x 254 mm
Themenwelt Naturwissenschaften Biologie Biochemie
Naturwissenschaften Biologie Mikrobiologie / Immunologie
Schlagworte amyloid pathologies • extracellular matrix proteins • protein self-assembly phenomena • Solid-State NMR • Spectroscopic
ISBN-10 1-4939-7809-8 / 1493978098
ISBN-13 978-1-4939-7809-0 / 9781493978090
Zustand Neuware
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