Protein aggregation / Douglas A. Stein, editor.

Format:

Book

Contributor:

Stein, Douglas A.

Series:

Protein science and engineering.

Microbiology research advances series.

Protein science and engineering

Microbiology research advances

Language:

English

Subjects (All):

Proteins--Denaturation.

Proteins.

Protein folding.

Physical Description:

1 online resource (312 p.)

Edition:

1st ed.

Place of Publication:

New York : Nova Biomedical Books, c2011.

Language Note:

English

Summary:

Protein aggregation is the aggregation of mis-folded proteins, and is thought to be responsible for many degenerative diseases, such as Alzheimer's. This book presents current research from across the globe in the study of protein aggregation, including the processes of protein aggregation induced by freezing and lyophilization; functional amyloids; thermally induced aggregation of a model system protein - insulin; the aggregation of albumin; synucleins implicated in neurodegenerative diseases and some forms of cancer; yeast protein aggregates; and the folding and aggregation features of proteins.

Contents:

Intro

PROTEIN AGGREGATION

Contents

Preface

Changes in Protein Structure under the Effects of Cryopreservation and Cryoprotective Agents

Abstract

Introduction

Cold Denaturation of Proteins

Disturbance of Protein Conformation Affected by Ice Formation

Disturbance of Protein Conformation Affected by Dehydration

Stabilizing Effects of Cryopotectant Agents on Proteins

Aggregation Frozen-Thawed and Frozen-Dried Proteins

Conclusion

References

Molecular Chaperones and Proteases as Suppressors of Protein Aggregation in Gram-Negative Bacteria

The Cytoplasmic Protein Quality Control Systems

Cytoplasmic Chaperones

Hsp70 System

Hsp60 System

HtpG (Hsp90)

sHsps

Hsp100

Protein Unfolding and Degradation

Proteolysis in the Bacterial Cytoplasm

Structural Features of AAA+ Proteases

Mechanisms of Substrate Recognition

Proteolysis as a Control Mechanism under Stressful Conditions

Role of Molecular Chaperones and Proteases in the Cytoplasmic Inclusion Bodies Processing

The Extracytoplasmic Protein Quality Control Systems

Skp

SurA

FkpA

Acid-Stress Chaperones HdeA and HdeB

Periplasmic Proteases

HtrA

Characterization of the Proteolytic Activity of HtrA

Characterization of the Chaperone Activity of HtrA

Other Extracytoplasmic Proteases

Expression of Recombinant Proteins in the Periplasm - Troubleshooting

Native Functions of Amyloid

1. Functional Amyloids

22. Bacteerial Ammyloid

2.1. Curli Fibrils

2.2. Pili of Mycobacterium Tuberculosis

2.3. Chaplin Fibrils

2.4. Microcin Amyloid

2.5. Harpins of Plant Pathogenic Bacteria

2.6. Endospore

2.7. Biofilms

2.8. Bacterial Inclusion Bodies Contain Amyloid Like Structure.

3. Fungal Amyloid

3.1. Hydrophobins

3.1.1. SC3 Hydrophobin

3.1.2. EAS of Neurospora Crassa

3.2. Adhesins of Yeast

4. Fungal Prions

4.1. Het-s amyloid in Podospora anserine

4.2. Yeast Prions

4.2.1. Amyloid of Ure2p in [URE3]

4.2.2. Amyloid of Sup35 in [PSI+]

4.2.3. Amyloid of Rnq1 in [PIN+]

5. Mammalian Functional Amyloid

5.1. Biogenesis of Mammalian Melanosome

5.1.1. Pmel Amyloid and Melanin Synthesis

5.2. Amyloid in Secretory Granules Biogenesis

6. Other Functional Amyloids

7. Functional vs Disease Amyloid

8. Conclusion and Future Direction

Acknowledgment

Nucleation Mechanisms and Morphologies in Insulin Amyloid Fibril Formation

1. Introduction

1.1. Nucleation Mechanisms in Protein Aggregation

1.1.1. Homogeneous and Secondary Nucleation

1.2. Model System, Experimental Approach and Aim of the Study

2. Results and Discussion

2.1. Human Insulin in Acetic Acid Solutions

2.1.1. Characterization of Fibril Formation

2.1.2. Correlation between FFV and 1/t50%

2.1.3. Statistical Study

2.2. Bovine insulin in HCl Solutions

2.2.1 Different Processes and Morphologies Occurring during the Fibrillation Kinetics

2.2.2. Lag Phase in the Low Concentration Regime

2.2.3. Initial Fibrils Growth in the Low Concentration Regime

Conclusions

Acknowledgments

On the Aggregation of Albumin: Influences of the Protein Glycation

Importance of Albumin in Human Physiology

Structural Aspect of Albumin

Albumin Aggregation

BSA Structural Modifications and Aggregation

Albumin Aggregation - Consequences of the Protein Glycation

Albumin Glycation Impact on Albumin Structure

Albumin Glycation is Characterized by Aggregates Growth

Glycated Albumin Showed Lower Propensity For Thermal Aggregation.

Conclusion

The Role of Conformational Domain Lability of Fibrinogen Molecules in Processes of Self-Assembly of Fibrin Monomers and Fibrinogen Aggregation

The Self-Assembly of the Single-Stranded Fibrin Protofibrils

Mechanism of Aggregation of Fibrinogen Molecules. The Influence of Fibrin-Stabilizing Factor

Structural Modification of Fibrinogen as a Result of Free-Radical Oxidation

Two Faced Members of the Family: The Synucleins

Physiological Functions of Synucleins

α-Synuclein

β-Synuclein

γ-Synuclein

Interaction of Amyloidogenic Proteins

Oxidized γ-synuclein is Toxic and Acts as an Antichaperone

Inclusion Bodies: A New Concept of Biocatalysts

Comparative Study of Bovine and Ovine Caseinate Aggregation Processes: Calcium-Induced Aggregation and Acid Aggregation

Colloidal Stability Test

Size Variations of the CCA

Analysis of Conformational and Surface Hydrophobicity Changes

Caseinate Acid Aggregation

Rheological Properties of Acid Gels

Protein Aggregation

Protein Aggregation and Neurodegenerative Disease

Protein Folding in Solution

Many Factors Affect the Protein Aggregation Process

Protein Aggregation and Cytotoxicity

Yeast Protein Aggregates, Containing Chaperones and Glucose Metabolism Enzymes

Materials and Methods

Strains and Pasmids

The Cultural Media and Basic Methods

Preparation and Analysis of Cell Lysate Pellets

Electrophoresis

Measuring Fluorescence Intensity

Model Experiments with Insulin Fibrils.

Red Pigment purification

Two-dimensional Polyacrylamide Gel Electrophoresis

Mass spectrometry and Protein Identification

Results

Folding and Aggregation Features of Proteins

Results and Discussion

A Description of the Database of Globular Proteins with Experimentally Determined Amyloidogenic Regions

Theoretical Search for Folding Nuclei of Amyloidogenic Proteins

Intersection of Experimentally Determined Amyloidogenic Regions with the Predicted Folding Nuclei

Creation of the Database of Amyloidogenic Proteins

Theoretical Search for Folding Nuclei

Calculation of Φ-Values

Statistical Tests

Funding

Chapter Sources

Index.

Notes:

Description based upon print version of record.

Includes bibliographical references and index.

ISBN:

1-61122-126-9

OCLC:

830323666