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E-raamat: Protein Aggregation in Bacteria - Functional and Structural Properties of Inclusion Bodies in Bacterial Cells: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells [Wiley Online]

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Editors Doglia and Lotti offer this compilation on bacterial protein aggregation via inclusion bodies. A detailed introduction to protein folding processes and dynamics opens the book, followed by chapters on recruitment of unfolding chaperones for use on misfolded recombinant proteins and use of osmolytes for chaperone activity. The relevance of inclusion bodies to amyloid aggregation and eukaryotic aggregation is discussed, as well as their structural properties and potential biomedical applications. Finally, recombinant protein aggregation as a production and design issue is addressed. Annotation ©2014 Ringgold, Inc., Portland, OR (protoview.com)

Focuses on the aggregation of recombinant proteins in bacterial cells in the form of inclusion bodies—and on their use in biotechnological and medical applications

The first book devoted specifically to the topic of aggregation in bacteria, Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells provides a large overview of protein folding and aggregation, including cell biology and methodological aspects. It summarizes, for the first time in one book, ideas and technical approaches that pave the way for a direct use of inclusion bodies in biotechnological and medical applications.

Protein Aggregation in Bacteria covers:

  • Molecular and cellular mechanisms of protein folding, aggregation, and disaggregation in bacteria
  • Physiological importance and consequences of aggregation for the bacterial cell
  • Factors inherent to the protein sequence responsible for aggregation and evolutionary mechanisms to keep proteins soluble
  • Structural properties of proteins expressed as soluble aggregates and as inclusion bodies within bacterial cells both from a methodological point of view and with regard to their similarity with amyloids
  • Control of the structural and functional properties of aggregated proteins and use thereof in biotechnology and medicine

Protein Aggregation in Bacteria is ideal for researchers in protein science, biochemistry, bioengineering, biophysics, microbiology, medicine, and biotechnology, particularly if they are related with the production of recombinant proteins and pharmaceutical science.

Contributors vii
Preface xi
Introduction to the Wiley Series in Protein and Peptide Science xiii
1 Fundamentals of Protein Folding
1(62)
Vladimir N. Uversky
2 Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins
63(14)
Rayees U.H. Mattoo
Pierre Goloubinoff
3 Osmolytes as Chemical Chaperones to Use in Protein Biotechnology
77(16)
Ario de Marco
4 Inclusion Bodies in the Study of Amyloid Aggregation
93(24)
Anna Villar-Pique
Salvador Ventura
5 Protein Aggregation in Unicellular Eukaryotes
117(34)
Marina Caldara
Joris Winderickx
Vanessa Franssens
6 Structural Properties of Bacterial Inclusion Bodies
151(30)
Antonino Natalello
Diletta Ami
Silvia Maria Doglia
7 Residue-Specific Structural Studies of Inclusion Bodies
181(22)
Christian Wasmer
Marielle Walti
Yongli Chen
Lei Wang
8 Biomedical Applications of Bacterial Inclusion Bodies
203(18)
Imma Ratera
Spela Peternel
Joaquin Seras-Franzoso
Olivia Cano-Garrido
Elena Garcia-Fruitos
Rafael Cubarsi
Esther Vazquez
Jose Luis Corchero
Escarlata Rodriguez-Carmona
Jaume Veciana
Antonio Villaverde
9 Aggregation of Recombinant Proteins: Understanding Basic Issues to Overcome Production Bottlenecks
221(26)
Marina Lotti
Loredano Pollegioni
10 Fusion to a Pull-Down Module: Designing Enzymes to Form Biocatalytically Active Insoluble Aggregates
247(16)
Bernd Nidetzky
Index 263
SILVIA MARIA DOGLIA, PhD, is Professor of Physics at the University of Milano-Bicocca, Italy. She received her Laurea degree in Physics at the University of Milano. She has been Staff Research Scientist of the Italian National Research Council; Visiting Scientist at the University of Stockholm; Visiting Professor at the Universities of Orléans (Fr) and of Reims (Fr). Her research in Biophysics at the University of Milano-Bicocca is focused on the study of protein folding and aggregation in vitro and in situ.

MARINA LOTTI, PhD, is Professor of Biochemistry at the University of Milano-Bicocca, Italy, where she leads the group Protein Engineering and Industrial Enzymology, and is the Head of the Department of Biotechnology and Biosciences. She obtained her PhD degree at the Max-Planck Institute of Molecular Genetics, Berlin, and was a researcher of the Italian National Research Council. Major research topics include the production of recombinant proteins, protein aggregation, cold-active enzymes, and intrinsically disordered proteins.