Bio-nanoimaging
Protein Misfolding and Aggregation
Published on 7. January 2014
Book
Hardback
552 pages
978-0-12-394431-3 (ISBN)
Description
Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering:
- Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits
- Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers
- Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide
Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties.
- Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits
- Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers
- Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide
Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties.
Reviews / Votes
"Among the topics are conformation-dependent antibodies as tools for characterizing amyloid protein aggregates, studying the molecular determinants of protein oligomerization in neurodegenerative disorders by bimolecular fluorence complimentation, possible function and toxicity of multiple oligomeric/conformational states of the globular protein human stefin B..." --ProtoView.com, February 2014More details
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Researchers and post-graduate students studying molecular medicine and molecular basis of disease, biotechnology, nanomedicine, pharmacology and drug discovery, molecular and cellular biology, biochemistry, biophysics, structural biology
Product notice
sewn/stitched
Paper over boards
Illustrations
Approx. 450 illustrations (200 in full color)
Dimensions
Height: 282 mm
Width: 222 mm
Thickness: 32 mm
Weight
1736 gr
ISBN-13
978-0-12-394431-3 (9780123944313)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
Additional editions
E-Book
01/2013
Elsevier
€155.00
Available for download
Persons
Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his PhD from Moscow Institute of Physics and Technology and D.Sc. from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. Since 2010, Professor Uversky has worked at University of South Florida, where he works on various aspects of protein intrinsic disorder phenomenon and analysis of protein folding and misfolding processes. He has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He also servs as an editor in a number of scientific journals.
Content
Part 1. Nanotechnology and nanoimaging of aggregating proteins
Nanoimaging of aggregated proteins; Cryoelectron microscopy of beta(2)-microglobulin; Amyloid fibril length quantification by AFM; Seeing fibril formation in real time; Studying amyloidogensis by FRET; Structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy; Analyzing amyloid fibril structure by scanning transmission electron microscopy; Magic angle spinning NMR of amyloid fibrils; Analyzing protein deposits in vivo by confocal laser multiphoton laser scanning microscopy; Amyloid imaging agents; Reporters of amyloid structure; Immunohistochemical detection of amyloid components; Scanning tunneling microscopy of protein deposits; Probing of protein misfolding with single molecule force spectroscopy; Single molecule characterization of ?-synuclein in aggregation-prone states
Part 2. Polymorphism of protein misfolded and aggregated species
Fibrillar polymorphism; Ab fibril polymorphism; Prefibrillar Ab oligomers; Structural heterogeneity of in vitro and ex vivo amyloid assemblies; Polymorphism of tau fibrils; Amyloid-like protofibrils with different physical properties; Micelle-Like Architecture of the Amyloid-? Peptide; Insulin oligomers; Worm-like amyloid fibrils of mouse prion protein; Apolipoprotein C-II Amyloid Fibrils; Amylin oligomers and fibrils; Amyloid fibrils of human stefins; Fibrillar structure of Sup35 in vivo; Dopamine-induced ?-synuclein oligomers ; Amyloid spherulites; A stable lipid-induced aggregate of alpha-synuclein
Part 3. Polymorphism of protein misfolding and aggregation processes
Multiple pathways of lysozyme aggregation; Structure-function study of amyloid ion channels in neurodegenerative diseases; Amyloid ?-protein assembly; Molecular mechanisms underlying alpha synucelin misassembly; Multiple pathways of amyloid assembly /disassembly studied by AFM; Sequestering of metastable proteins with essential cellular functions by amyloid-like aggregates; Misfolded intermediate of a PDZ domain; Structural characterization of the amyloidogenic state of human lysozyme; Landscape Model of Filamentous Protein Aggregation; Micelle formation by human islet amyloid polypeptide; Effect of anionic polysaccharide on ?-lactoglobulin fibrillation
Nanoimaging of aggregated proteins; Cryoelectron microscopy of beta(2)-microglobulin; Amyloid fibril length quantification by AFM; Seeing fibril formation in real time; Studying amyloidogensis by FRET; Structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy; Analyzing amyloid fibril structure by scanning transmission electron microscopy; Magic angle spinning NMR of amyloid fibrils; Analyzing protein deposits in vivo by confocal laser multiphoton laser scanning microscopy; Amyloid imaging agents; Reporters of amyloid structure; Immunohistochemical detection of amyloid components; Scanning tunneling microscopy of protein deposits; Probing of protein misfolding with single molecule force spectroscopy; Single molecule characterization of ?-synuclein in aggregation-prone states
Part 2. Polymorphism of protein misfolded and aggregated species
Fibrillar polymorphism; Ab fibril polymorphism; Prefibrillar Ab oligomers; Structural heterogeneity of in vitro and ex vivo amyloid assemblies; Polymorphism of tau fibrils; Amyloid-like protofibrils with different physical properties; Micelle-Like Architecture of the Amyloid-? Peptide; Insulin oligomers; Worm-like amyloid fibrils of mouse prion protein; Apolipoprotein C-II Amyloid Fibrils; Amylin oligomers and fibrils; Amyloid fibrils of human stefins; Fibrillar structure of Sup35 in vivo; Dopamine-induced ?-synuclein oligomers ; Amyloid spherulites; A stable lipid-induced aggregate of alpha-synuclein
Part 3. Polymorphism of protein misfolding and aggregation processes
Multiple pathways of lysozyme aggregation; Structure-function study of amyloid ion channels in neurodegenerative diseases; Amyloid ?-protein assembly; Molecular mechanisms underlying alpha synucelin misassembly; Multiple pathways of amyloid assembly /disassembly studied by AFM; Sequestering of metastable proteins with essential cellular functions by amyloid-like aggregates; Misfolded intermediate of a PDZ domain; Structural characterization of the amyloidogenic state of human lysozyme; Landscape Model of Filamentous Protein Aggregation; Micelle formation by human islet amyloid polypeptide; Effect of anionic polysaccharide on ?-lactoglobulin fibrillation