Javascript must be enabled to continue!
Structural Analysis of Fibrous Proteins
View through CrossRef
AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionOverview: Protein Fibers Formedin vivoAmyloid FibersSilksCollagensActin, Myosin, and Tropomyosin FilamentsIntermediate Filaments/Nuclear LaminaFibrinogen/FibrinMicrotubulesElastic FibersFlagella and PiliFilamentary Structures in Rod‐like VirusesProtein Fibers Used by Viruses and Bacteriophages to Bind to Their HostsOverview: Fiber StructuresStudy of the Structure of β‐sheet‐containing ProteinsAmyloidPaired Helical Filamentsβ‐Silksβ‐Sheet‐containing Viral Fibersα‐Helix‐containing Protein FibersCollagenTropomyosinIntermediate FilamentsProtein Polymers Consisting of a Mixture of Secondary StructureTubulinActin and Myosin FilamentsMethods to Study Fiber AssemblyCircular Dichroism Measurements for Monitoring Structural Changes Upon Fiber AssemblyTheory of CDExperimental Guide to Measure CD Spectra and Structural Transition KineticsIntrinsic Fluorescence Measurements to Analyze Structural ChangesTheory of Protein FluorescenceExperimental Guide to Measure Trp FluorescenceCovalent Fluorescent Labeling to Determine Structural Changes of Proteins with Environmentally Sensitive FluorophoresTheory on Environmental Sensitivity of FluorophoresExperimental Guide to Labeling Proteins With Fluorophores1‐Anilino‐8‐Naphthalensulfonate (ANS) Binding to Investigate Fiber AssemblyTheory on UsingANSFluorescence for Detecting Conformational Changes in ProteinsExperimental Guide to UsingANSfor Monitoring Protein Fiber AssemblyLight Scattering to Monitor Particle GrowthTheory of Classical Light ScatteringTheory of Dynamic Light ScatteringExperimental Guide to Analyzing Fiber Assembly UsingDLSField‐flow Fractionation to Monitor Particle GrowthTheory ofFFFExperimental Guide to UsingFFFfor Monitoring Fiber AssemblyFiber Growth‐rate Analysis Using Surface Plasmon ResonanceTheory ofSPRExperimental Guide to UsingSPRfor Fiber‐growth AnalysisSingle‐fiber Growth Imaging Using Atomic Force MicroscopyTheory of Atomic Force MicroscopyExperimental Guide for UsingAFMto Investigate Fiber GrowthDyes Specific for Detecting Amyloid FibersTheory on Congo Red and ThioflavinTBinding to AmyloidExperimental Guide to Detecting Amyloid Fibers withCRand Thioflavin BindingMethods to Study Fiber Morphology and StructureScanning Electron Microscopy for Examining the Low‐resolution Morphology of a Fiber SpecimenTheory ofSEMExperimental Guide to Examining Fibers bySEMTransmission Electron Microscopy for Examining Fiber Morphology and StructureTheory ofTEMExperimental Guide to Examining Fiber Samples byTEMCryo‐electron Microscopy for Examination of the Structure of Fibrous ProteinsTheory of Cryo‐electron MicroscopyExperimental Guide to Preparing Proteins for Cryo‐electron MicroscopyStructural Analysis from Electron MicrographsAtomic Force Microscopy for Examining the Structure and Morphology of Fibrous ProteinsExperimental Guide for UsingAFMto Monitor Fiber MorphologyUse ofX‐ray Diffraction for Examining the Structure of Fibrous ProteinsTheory ofX‐Ray Fiber DiffractionExperimental Guide toX‐Ray Fiber DiffractionFourier Transformed Infrared SpectroscopyTheory ofFTIRExperimental Guide to Determining Protein Conformation byFTIRConclusionsAcknowledgements
Title: Structural Analysis of Fibrous Proteins
Description:
AbstractOriginally published in: Protein Folding Handbook.
Part II.
Edited by Johannes Buchner and Thomas Kiefhaber.
Copyright © 2005 Wiley‐VCH Verlag GmbH & Co.
KGaA Weinheim.
Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionOverview: Protein Fibers Formedin vivoAmyloid FibersSilksCollagensActin, Myosin, and Tropomyosin FilamentsIntermediate Filaments/Nuclear LaminaFibrinogen/FibrinMicrotubulesElastic FibersFlagella and PiliFilamentary Structures in Rod‐like VirusesProtein Fibers Used by Viruses and Bacteriophages to Bind to Their HostsOverview: Fiber StructuresStudy of the Structure of β‐sheet‐containing ProteinsAmyloidPaired Helical Filamentsβ‐Silksβ‐Sheet‐containing Viral Fibersα‐Helix‐containing Protein FibersCollagenTropomyosinIntermediate FilamentsProtein Polymers Consisting of a Mixture of Secondary StructureTubulinActin and Myosin FilamentsMethods to Study Fiber AssemblyCircular Dichroism Measurements for Monitoring Structural Changes Upon Fiber AssemblyTheory of CDExperimental Guide to Measure CD Spectra and Structural Transition KineticsIntrinsic Fluorescence Measurements to Analyze Structural ChangesTheory of Protein FluorescenceExperimental Guide to Measure Trp FluorescenceCovalent Fluorescent Labeling to Determine Structural Changes of Proteins with Environmentally Sensitive FluorophoresTheory on Environmental Sensitivity of FluorophoresExperimental Guide to Labeling Proteins With Fluorophores1‐Anilino‐8‐Naphthalensulfonate (ANS) Binding to Investigate Fiber AssemblyTheory on UsingANSFluorescence for Detecting Conformational Changes in ProteinsExperimental Guide to UsingANSfor Monitoring Protein Fiber AssemblyLight Scattering to Monitor Particle GrowthTheory of Classical Light ScatteringTheory of Dynamic Light ScatteringExperimental Guide to Analyzing Fiber Assembly UsingDLSField‐flow Fractionation to Monitor Particle GrowthTheory ofFFFExperimental Guide to UsingFFFfor Monitoring Fiber AssemblyFiber Growth‐rate Analysis Using Surface Plasmon ResonanceTheory ofSPRExperimental Guide to UsingSPRfor Fiber‐growth AnalysisSingle‐fiber Growth Imaging Using Atomic Force MicroscopyTheory of Atomic Force MicroscopyExperimental Guide for UsingAFMto Investigate Fiber GrowthDyes Specific for Detecting Amyloid FibersTheory on Congo Red and ThioflavinTBinding to AmyloidExperimental Guide to Detecting Amyloid Fibers withCRand Thioflavin BindingMethods to Study Fiber Morphology and StructureScanning Electron Microscopy for Examining the Low‐resolution Morphology of a Fiber SpecimenTheory ofSEMExperimental Guide to Examining Fibers bySEMTransmission Electron Microscopy for Examining Fiber Morphology and StructureTheory ofTEMExperimental Guide to Examining Fiber Samples byTEMCryo‐electron Microscopy for Examination of the Structure of Fibrous ProteinsTheory of Cryo‐electron MicroscopyExperimental Guide to Preparing Proteins for Cryo‐electron MicroscopyStructural Analysis from Electron MicrographsAtomic Force Microscopy for Examining the Structure and Morphology of Fibrous ProteinsExperimental Guide for UsingAFMto Monitor Fiber MorphologyUse ofX‐ray Diffraction for Examining the Structure of Fibrous ProteinsTheory ofX‐Ray Fiber DiffractionExperimental Guide toX‐Ray Fiber DiffractionFourier Transformed Infrared SpectroscopyTheory ofFTIRExperimental Guide to Determining Protein Conformation byFTIRConclusionsAcknowledgements.
Related Results
Form Follows Force: A theoretical framework for Structural Morphology, and Form-Finding research on shell structures
Form Follows Force: A theoretical framework for Structural Morphology, and Form-Finding research on shell structures
The springing up of freeform architecture and structures introduces many challenges to structural engineers. The main challenge is to generate structural forms with high structural...
Characterization and classification of unregulated mineral fibers: The case of fibrous datolite from Rio Manubiola Valley, Parma, Italy
Characterization and classification of unregulated mineral fibers: The case of fibrous datolite from Rio Manubiola Valley, Parma, Italy
Abstract
The widespread presence of mineral fibers necessitates their thorough identification, characterization, and assessment of potential health effects. This ...
Periprosthetic Tissue Removal in Minimally Invasive Hip Refix Procedures
Periprosthetic Tissue Removal in Minimally Invasive Hip Refix Procedures
An alternative to conventional revision surgery of loosened hip prostheses is a new minimally invasive refixation procedure. This procedure requires the removal of periprosthetic f...
Global Landscape of Structural Proteins of Infectious Spleen and Kidney Necrosis Virus
Global Landscape of Structural Proteins of Infectious Spleen and Kidney Necrosis Virus
ABSTRACT
Infectious spleen and kidney necrosis virus
(ISKNV), the type species of the genus
Megalocytivirus
in the family...
Section-level genome sequencing and comparative genomics of Aspergillus sections Cavernicolus and Usti
Section-level genome sequencing and comparative genomics of Aspergillus sections Cavernicolus and Usti
Fig. S1. A cladogram representation of the phylogenetic relations between the species in this paper. The red labels show bootstrap values of 100 % and the black labels show bootstr...
Identification and characterization of CFEM Proteins from Phakopsora pachyrhizi, the Asian soybean rust fungus
Identification and characterization of CFEM Proteins from Phakopsora pachyrhizi, the Asian soybean rust fungus
Asian soybean rust (ASR) caused by the fungus Phakopsora pachyrhizi is one of the main fungal diseases of soybean, which can cause losses of up to 95% of production under favorable...
Identification of heparin‐binding proteins in bovine seminal plasma
Identification of heparin‐binding proteins in bovine seminal plasma
AbstractA group of four similar proteins, BSP‐A1, BSP‐A2, BSP‐A3, and BSP‐30‐kDa, represent the major acidic proteins found in bovine seminal plasma (BSP). These proteins are secre...
The Puf family of RNA-binding proteins in plants: phylogeny, structural modeling, activity and subcellular localization
The Puf family of RNA-binding proteins in plants: phylogeny, structural modeling, activity and subcellular localization
Abstract
Background
Puf proteins have important roles in controlling gene expression at the post-transcriptional level by promoting RNA decay and...

