bluuebunny/crossref_metadata_2025_split huggingface dataset:
13C‐ and15N‐Isotopic Labeling of Proteins
Authors: Klammt Christian , Bernhard Frank , Rüterjans Heinz 
Published: March 2008

AbstractOriginally published in: Molecular Biology in Medicinal Chemistry. Edited by Theodor Dingermann, Dieter Steinhilber and Gerd Folkers. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30431‐8The sections in this article areIntroductionExpression Systems for theIn VivoIncorporation of13C and15N Labels into ProteinsProtein Production and13C and15N‐labeling inE. coliExpression Systems13C‐ and15N‐labeling of Proteins inP. pastoris13C‐ and15N‐labeling of Proteins by Expression in Chinese Hamster Ovary (CHO) Cells13C‐ and15N‐labeling of Proteins in Other OrganismsStrategies for the Production of Selectively13C‐ and15N‐labeled ProteinsSelective Labeling of Amino AcidsSpecific Isotope Labeling with13CSegmental Isotope LabelingCell‐free Isotope LabelingComponents of Cell‐free Expression SystemsCell‐free Expression TechniquesSpecific Applications of the Cell‐free Labeling Technique
Studying Protein Folding and Aggregation by Laser Light Scattering
Authors: Gast Klaus , Modler Andreas J. 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionBasic Principles of Laser Light ScatteringLight Scattering by Macromolecular SolutionsMolecular Parameters Obtained from Static Light Scattering (SLS)Molecular Parameters Obtained from Dynamic Light Scattering (DLS)Advantages of Combined SLS and DLS ExperimentsLaser Light Scattering of Proteins in Different Conformational States – Equilibrium Folding/Unfolding TransitionsGeneral Considerations, Hydrodynamic Dimensions in the Natively Folded StateChanges in the Hydrodynamic Dimensions during Heat‐induced UnfoldingChanges in the Hydrodynamic Dimensions upon Cold DenaturationDenaturant‐induced Changes of the Hydrodynamic DimensionsAcid‐induced Changes of the Hydrodynamic DimensionsDimensions in Partially Folded States – Molten Globules and StatesComparison of the Dimensions of Proteins in Different Conformational StatesScaling Laws for the Native and Highly Unfolded States, Hydrodynamic ModelingStudying Folding Kinetics by Laser Light ScatteringGeneral Considerations, Attainable Time RegionsHydrodynamic Dimensions of the Kinetic Molten Globule of Bovine α‐LactalbuminRNase A is Only Weakly Collapsed During the Burst Phase of FoldingMisfolding and Aggregation Studied by Laser Light ScatteringOverview: Some Typical Light Scattering Studies of Protein AggregationStudying Misfolding and Amyloid Formation by Laser Light ScatteringOverview: Initial States, Critical Oligomers, Protofibrils, FibrilsAggregation Kinetics of Aβ PeptidesKinetics of Oligomer and Fibril Formation of PGK and Recombinant Hamster Prion ProteinMechanisms of Misfolding and Misassembly, Some General RemarksProtocols and InstrumentationLaser Light Scattering InstrumentationBasic Experimental Set‐up, General RequirementsSupplementary Measurements and Useful OptionsCommercially Available Light Scattering InstrumentationExperimental Protocols for the Determination of Molecular Mass and Stokes Radius of a Protein in a Particular Conformational StateAcknowledgments
Spectroscopic Techniques to Study Protein Conformation
Authors: Schmid Franz 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag Gmbh & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2IntroductionAbsorbanceAbsorbance of ProteinsPractical Considerations for the Measurement of Protein AbsorbanceData InterpretationFluorescenceThe Fluorescence of ProteinsEnergy Transfer and Fluorescence Quenching in a Protein: BarnaseProtein Unfolding Monitored by FluorescenceEnvironmental Effects on Tyrosine and Tryptophan EmissionPractical ConsiderationsCircular DichroismCD Spectra of Native and Unfolded ProteinsMeasurement of Circular DichroismEvaluation of CD Data
Ion Channel Structural Studies
Authors: Bass Randal B. , Spencer Robert H. 
Published: March 2008

Abstract
Originally published in: Expression and Analysis of Recombinant Ions Channels. Edited by Jeffrey J. Clare and Derek J. Trezise. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31209‐2
The sections in this article are

Introduction

Expression of Membrane Proteins for Structural Studies

Mammalian Expression

Insect Expression

Yeast Expression

Bacterial Expression

The Detergent Factor

Purification

Crystallization

Use of Antibody Fragments

Generation of First Diffraction Datasets

Selenomethionine Phasing of Membrane Proteins

MAD
Phasing and Edge Scanning

Negative
B
‐factor Application (Structure Factor Sharpening)

Conclusions
Computational Analysis of Modular Protein Architectures
Authors: Linding Rune , Letunic Ivica , Gibson Toby J. , Bork Peer 
Published: March 2008

Abstract
Originally published in: Modular Protein Domains. Edited by Giovanni Cesareni, Mario Gimona, Marius Sudol and Michael Yaffe. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30813‐2
The sections in this article are

Introduction

Protein Architecture: Sequence, Structure, and Function

The Modular Model of Protein Function

Partitioning of Protein Space

Analyzing Globular Domains

Globularity of Domains

Resources for Analysis of Globular Domains

SMART: Simple Modular Architecture Research Tool

The SMART Alignment Set

SMART Relational Database System

Web Interface

Application of SMART

Other Features and Resources

Globular Repeats

Domain Interaction Prediction

No Domains?

Analyzing Nonglobular Protein Segments

Unstructured Regions: Protein Disorder

What Role Does Protein Disorder Play in Biology?

What is Protein Disorder?

Methods for Finding Protein Disorder

GlobPlotting

Prediction of Multiple Types of Disorder with DisEMBL

Design of Protein Expression Vectors

Function Prediction for Nonglobular Protein Segments

Available Resources

The Eukaryotic Linear Motif Resource: ELM

ELM
Annotation – ‘Site seeing’

ELM Resource Architecture

Knowledge‐based Decision Support (KBDS): ELM Filtering

Using ELM

URLs

Conclusions

Acknowledgements
Mass Spectrometry for the Detection and Identification of Proteins
Authors: König Simone , Haberland Jörg , Grote Jens , Zeller Martin , Gedig Erk , Fobker Manfred , Erren Michael , Pursley Stephen W. , Pearl John E. , Cullen Paul , Lorkowski Stefan 
Published: March 2008

AbstractOriginally published in: Analysing Gene Expression. Edited by Stefan Lorkowski, Paul Cullen. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30488‐2The sections in this article areIntroductionHow does mass spectrometry work?Ionisation of moleculesDetection of ionsAppearance of spectraModes of operationProteomic mass spectrometryData analysis tools for mass spectroscopic experimentsProteomics servers and databasesAn example: Identification of an isolated and unknown proteinIs quantification possible with mass spectrometry?Analysis of protein modificationsPhosphorylationGlycosylationAccess to protein tertiary structureAnalysis of intact proteins and non‐covalent protein complexesAffinity mass spectrometryConclusion
Protein Microarrays
Authors: König Simone , Haberland Jörg , Grote Jens , Zeller Martin , Gedig Erk , Fobker Manfred , Erren Michael , Pursley Stephen W. , Pearl John E. , Cullen Paul , Lorkowski Stefan 
Published: March 2008

AbstractOriginally published in: Analysing Gene Expression. Edited by Stefan Lorkowski, Paul Cullen. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30488‐2The sections in this article areIntroductionPrinciples and basics, typical results and applicationsConclusion
Separation Strategies for Proteomics
Authors: König Simone , Haberland Jörg , Grote Jens , Zeller Martin , Gedig Erk , Fobker Manfred , Erren Michael , Pursley Stephen W. , Pearl John E. , Cullen Paul , Lorkowski Stefan 
Published: March 2008

AbstractOriginally published in: Analysing Gene Expression. Edited by Stefan Lorkowski, Paul Cullen. Copyright © 2003 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30488‐2The sections in this article areIntroductionConventional slab gel electrophoresisIsoelectric focusing (IEF)Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) and Western blottingTwo‐dimensional polyacrylamide gel electrophoresis (2D‐PAGE)Two‐dimensional difference gel electrophoresis (2D‐DIGE)High‐performance liquid chromatography (HPLC)Ion exchange chromatography (IEC)Size exclusion chromatography (SEC)Affinity chromatographyReverse phase chromatography (RPC)Normal phase chromatographyCapillary electrophoresis (CE) and capillary electrochromatography (CEC)Multi‐dimensional separationsNew approachesIsotope‐coded affinity tag method (ICAT™)Multi‐epitope ligand‐Kartographie (MELK)Conclusion
Denaturation of Proteins by Urea and Guanidine Hydrochloride
Authors: Pace C. Nick , Grimsley Gerald R. , Scholtz J. Martin 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2

Introduction

How Urea Denatures Proteins

Linear Extrapolation Method

Δ
G
(H
2
O)

m
‐Values

Conclusions

Practical Considerations

How to Choose the Best Denaturant for your Study

How to Prepare Denaturant Solutions

Preparation of a urea stock solution

How to Determine Solvent Denaturation Curves

Determining a Urea or GdmCl Denaturation Curve

How to Analyze Urea or GdmCl Denaturant Curves

Determining Differences in Stability

Acknowledgments
Thermal Unfolding of Proteins
Authors: Makhatadze George I. 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionTwo‐state UnfoldingCold DenaturationMechanisms of ThermostabilizationThermodynamic Dissection of Forces Contributing to Protein StabilityHeat Capacity Changes, ΔCpEnthalpy of Unfolding, ΔHEntropy of Unfolding, ΔSMultistate TransitionsTwo‐state Dimeric ModelTwo‐state Multimeric ModelThree‐state Dimeric ModelTwo‐state Model with Ligand BindingFour‐state (Two‐domain Protein) ModelDifferential Scanning Calorimetry (DSC)How to Prepare forDSCExperimentsHow to Choose Appropriate ConditionsCritical Factors in RunningDSCExperiments
Pressure‐Temperature Phase Diagrams of Proteins
Authors: Doster Wolfgang , Friedrich Josef 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionBasic Aspects of Phase Diagrams of Proteins and Early ExperimentsThermodynamics of Pressure–Temperature Phase DiagramsMeasuring Phase Stability Boundaries with Optical TechniquesFluorescence Experiments with CytochromecResultsWhat Do We Learn from the Stability Diagram?ThermodynamicsDetermination of the Equilibrium Constant of DenaturationMicroscopic AspectsStructural Features of the Pressure‐denatured StateConclusions and OutlookAcknowledgment
Conformational Properties of Unfolded Proteins
Authors: Fleming Patrick J. , Rose George D. 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionUnfolded vs. Denatured ProteinsEarly HistoryThe Random CoilThe Random Coil–TheoryThe Random Coil Model Prompts Three QuestionsThe Folding FunnelTransition State TheoryOther ExamplesImplicit Assumptions from the Random Coil ModelThe Random Coil–ExperimentIntrinsic ViscositySAXSandSANSQuestions about the Random Coil ModelQuestions from TheoryTheFlory Isolated‐pair HypothesisStructure vs. Energy DualityThe “Rediscovery” of Polyproline II ConformationPIIin Unfolded Peptides and ProteinsQuestions from ExperimentResidual Structure in Denatured Proteins and PeptidesThe Reconciliation ProblemOrganization in the Unfolded State – the Entropic ConjectureSteric Restrictions beyond the DipeptideFuture DirectionsAcknowledgments
Kinetic Mechanisms in Protein Folding
Authors: Bachmann Annett , Kiefhaber Thomas 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionAnalysis of Protein Folding Reactions using Simple Kinetic ModelsGeneral Treatment of Kinetic DataTwo‐state Protein FoldingComplex Folding KineticsHeterogeneity in the Unfolded StateFolding through IntermediatesRapid Pre‐equilibriaFolding through an On‐pathway High‐energy IntermediateA Case Study: the Mechanism of Lysozyme FoldingLysozyme Folding atpH5.2 and Low Salt ConcentrationsLysozyme Folding at pH 9.2 or at High Salt ConcentrationsNon‐exponential KineticsConclusions and OutlookProtocols–Analytical Solutions of Three‐state Protein Folding ModelsTriangular MechanismOn‐pathway IntermediateOff‐pathway MechanismFolding Through an On‐pathway High‐Energy IntermediateAcknowledgments
Association and Folding of Small Oligomeric Proteins
Authors: Bosshard Hans‐Rudolf 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part I. 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 areIntroductionExperimental Methods Used to Follow the Folding of Oligomeric ProteinsEquilibrium MethodsKinetic MethodsDimeric ProteinsTwo‐state Folding of Dimeric ProteinsExamples of Dimeric Proteins Obeying Two‐state FoldingFolding of Dimeric Proteins through Intermediate StatesTrimeric and Tetrameric ProteinsConclusionsAppendix–Concurrent Association and Folding of Small Oligomeric ProteinsEquilibrium Constants for Two‐state FoldingHomooligomeric ProteinHeterooligomeric ProteinCalculation of Thermodynamic Parameters from Equilibrium ConstantsBasic Thermodynamic RelationshipsLinear Extrapolation of Denaturant Unfolding Curves of Two‐state ReactionCalculation of the van't Hoff Enthalpy Change from Thermal Unfolding DataCalculation of the van't Hoff Enthalpy Change from the Concentration‐dependence ofTmExtrapolation of Thermodynamic Parameters to Different Temperatures:Gibbs‐Helmholtz EquationKinetics of Reversible Two‐state Folding and Unfolding: Integrated Rate EquationsTwo‐state Folding of Dimeric ProteinTwo‐state Unfolding of Dimeric ProteinReversible Two‐state Folding and UnfoldingHomodimeric proteinHeterodimeric proteinKinetics of Reversible Two‐state Folding: Relaxation after Disturbance of a Preexisting Equilibrium (Method ofBernasconi)Acknowledgments
Disulfide Bond Formation in Prokaryotes
Authors: Collet Jean‐Francois , Bardwell James C. 
Published: March 2008

Abstract
Originally 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: 3‐527‐30784‐2
The sections in this article are

Introduction

Disulfide Bond Formation in the

E
.
coli

Periplasm

A Small Bond, a Big Effect

Disulfide Bond Formation Is a Catalyzed Process

Dsb
A
, a Protein‐folding Catalyst

How is
Dsb
A
Re‐oxidized?

From Where Does the Oxidative Power of
Dsb
B
Originate?

How Are Disulfide Bonds Transferred From
Dsb
B
to
Dsb
A
?

How Can
Dsb
B
Generate Disulfide by Quinone Reduction?

Disulfide Bond Isomerization

The Protein Disulfide Isomerases
Dsb
C
and
Dsb
G

Dimerization of
Dsb
C
and
Dsb
G
Is Important for Isomerase and Chaperone Activity

Dimerization Protects from
Dsb
B
Oxidation

Import of Electrons from the Cytoplasm:
Dsb
D

Conclusions
Folding of Membrane Proteins
Authors: Tamm Lukas K. , Hong Heedeok 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

Thermodyamics of Residue Partitioning into Lipid Bilayers

Stability of β‐Barrel Proteins

Stability of Helical Membrane Proteins

Helix and Other Lateral Interactions in Membrane Proteins

The Membrane Interface as an Important Contributor to Membrane Protein Folding

Membrane Toxins as Models for Helical Membrane Protein Insertion

Mechanisms of β‐Barrel Membrane Protein Folding

Experimental Protocols

SDS Gel Shift Assay for Heat‐modifiable Membrane Proteins

Reversible Folding and Unfolding Protocol Using OmpA as an Example

Tryptophan Fluorescence and Time‐resolved Distance Determination by Tryptophan Fluorescence Quenching

TDFQ Protocol for Monitoring the Translocation of Tryptophans across Membranes

Circular Dichroism Spectroscopy

Fourier Transform Infrared Spectroscopy

Protocol for Obtaining Conformation and Orientation of Membrane Proteins and Peptides by Polarized ATR‐FTIR Spectroscopy

Acknowledgments
Molecular Dynamics Simulations to Study Protein Folding and Unfolding
Authors: Caflisch Amedeo , Paci Emanuele 
Published: March 2008

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 areIntroductionMolecular Dynamics Simulations of Peptides and ProteinsFolding of Structured PeptidesReversible Folding and Free Energy SurfacesNon‐Arrhenius Temperature Dependence of the Folding RateDenatured State and Levinthal ParadoxFolding Events of Trp‐cageUnfolding Simulations of ProteinsHigh‐temperature SimulationsBiased UnfoldingForced UnfoldingDetermination of the Transition State EnsembleMD Techniques and ProtocolsTechniques to Improve SamplingReplica Exchange Molecular DynamicsMethods Based on Path SamplingMD with RestraintsDistributed Computing ApproachImplicit Solvent Models versus Explicit WaterConclusion
Molecular Dynamics Simulations of Proteins and Peptides
Authors: Tavan Paul , Carstens Heiko , Mathias Gerald 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

Basic Physics of Protein Structure and Dynamics

Protein Electrostatics

Relaxation Times and Spatial Scales

Solvent Environment

Water

Polarizability of the Peptide Groups and of Other Protein Components

State of the Art

Control of Thermodynamic Conditions

Long‐range Electrostatics

Polarizability

Higher Multipole Moments of the Molecular Components

MM Models of Water

Complexity of Protein–Solvent Systems and Consequences for MM‐MD

What about Successes of MD Methods?

Accessible Time Scales and Accuracy Issues

Continuum Solvent Models

Are there Further Problems beyond Electrostatics and Structure Prediction?

Conformational Dynamics of a Light‐switchable Model Peptide

Computational Methods

Results and Discussion

Summary

Acknowledgments
Electrostatics of Proteins: Principles, Models and Applications
Authors: Braun‐Sand Sonja , Warshel Arieh 
Published: March 2008

Abstract
Originally published in: Protein Folding Handbook. Part I. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag Gmbh & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2
The sections in this article are

Introduction

Historical Perspectives

Electrostatic Models: From Microscopic to Macroscopic Models

All‐Atom Models

Dipolar Lattice Models and the PDLD Approach

The PDLD/S‐LRA Model

Continuum (Poisson‐Boltzmann) and Related Approaches

Effective Dielectric Constant for Charge–charge Interactions and the GB Model

The Meaning and Use of the Protein Dielectric Constant

Validation Studies

Systems Studied

Solvation Energies of Small Molecules

Calculation of p
K
a
Values of Ionizable Residues

Redox and Electron Transport Processes

Ligand Binding

Enzyme Catalysis

Ion Pairs

Protein‐Protein Interactions

Ion Channels

Helix Macrodipoles versus Localized Molecular Dipoles

Folding and Stability

Conclusions

Acknowledgments
Folding and Association of Multi‐domain and Oligomeric
Authors: Lilie Hauke , Seckler Robert 
Published: March 2008

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 areIntroductionFolding of Multi‐domain ProteinsDomain Architectureγ‐Crystallin as a Model for a Two‐domain ProteinThe Giant Protein TitinFolding and Association of Oligomeric ProteinsWhy Oligomers?Inter‐subunit InterfacesDomain SwappingStability of Oligomeric ProteinsMethods Probing Folding/AssociationChemical Cross‐linkingAnalytical Gel Filtration ChromatographyScattering MethodsFluorescence Resonance Energy TransferHybrid FormationKinetics of Folding and AssociationGeneral ConsiderationsReconstitution IntermediatesRates of AssociationHomo‐ versus HeterodimerizationRenaturation versus AggregationCase Studies on Protein Folding and AssociationAntibody FragmentsTrimeric Tail Spike Protein of BacteriophageP22
Chaperone Function in Vitro
Authors: Buchner Johannes , Walter Stefan 
Published: March 2008

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 areIntroductionBasic Functional Principles of Molecular ChaperonesRecognition of Nonnative ProteinsInduction of Conformational Changes in the SubstrateEnergy Consumption and Regulation of Chaperone FunctionLimits and Extensions of the Chaperone ConceptCo‐chaperonesSpecific ChaperonesWorking with Molecular ChaperonesNatural versus Artificial Substrate ProteinsStability of ChaperonesAcknowledgments
Peptidyl‐prolylcis/transIsomerases
Authors: Fischer Gunter 
Published: March 2008

AbstractOriginally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2The sections in this article areIntroductionPeptidyl‐prolylcis/transIsomerizationMonitoring Peptidyl‐prolylcis/transIsomerase ActivityPrototypical Peptidyl‐prolylcis/transIsomerasesGeneral ConsiderationsPrototypic CyclophilinsPrototypicFK506‐binding ProteinsPrototypic ParvulinsConclusions
Proteins Import into Mitochondria
Authors: Neupert Walter , Brunner Michael , Hell Kai 
Published: March 2008

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 areIntroductionTranslocation Machineries and Pathways of the Mitochondrial Protein Import SystemImport of Proteins Destined for the Mitochondrial MatrixImport into Mitochondria Requires Protein UnfoldingMechanisms of Unfolding by the Mitochondrial Import MotorTargeted Brownian RatchetPower‐stroke ModelStudies to Discriminate between the ModelsStudies on the Unfolding of PreproteinsComparison of the Import of Folded and Unfolded ProteinsImport of Preproteins With Different Presequence LengthsImport of Titin DomainsUnfolding by the Mitochondrial Membrane Potential ΔΨMechanistic Studies of the Import MotorBrownian Movement of the Polypeptide Within the Import ChannelRecruitment of mtHsp70 by Tim44Import Without Recruitment of mtHsp70 by Tim44MtHsp70 Function in the Import MotorConclusions