Protein and Peptide Folding, Misfolding, and Non-Folding / Wiley Series in Protein and Peptide Science (ePub)
(Sprache: Englisch)
Sheds new light on intrinsically disordered proteins and
peptides, including their role in neurodegenerative diseases
With the discovery of intrinsically disordered proteins and
peptides (IDPs), researchers realized that proteins do not
necessarily...
peptides, including their role in neurodegenerative diseases
With the discovery of intrinsically disordered proteins and
peptides (IDPs), researchers realized that proteins do not
necessarily...
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Produktinformationen zu „Protein and Peptide Folding, Misfolding, and Non-Folding / Wiley Series in Protein and Peptide Science (ePub)“
Sheds new light on intrinsically disordered proteins and
peptides, including their role in neurodegenerative diseases
With the discovery of intrinsically disordered proteins and
peptides (IDPs), researchers realized that proteins do not
necessarily adopt a well defined secondary and tertiary structure
in order to perform biological functions. In fact, IDPs play
biologically relevant roles, acting as inhibitors, scavengers, and
even facilitating DNA/RNA-protein interactions. Due to their
propensity for self-aggregation and fibril formation, some IDPs are
involved in neurodegenerative diseases such as Parkinson's and
Alzheimer's.
With contributions from leading researchers, this text reviews
the most recent studies, encapsulating our understanding of IDPs.
The authors explain how the growing body of IDP research is
building our knowledge of the folding process, the binding of
ligands to receptor molecules, and peptide self-aggregation.
Readers will discover a variety of experimental, theoretical, and
computational approaches used to better understand the properties
and function of IDPs. Moreover, they'll discover the role of IDPs
in human disease and as drug targets.
Protein and Peptide Folding, Misfolding, and Non-Folding begins
with an introduction that explains why research on IDPs has
significantly expanded in the past few years. Next, the book is
divided into three sections:
* Conformational Analysis of Unfolded States
* Disordered Peptides and Molecular Recognition
* Aggregation of Disordered Peptides
Throughout the book, detailed figures help readers understand
the structure, properties, and function of IDPs. References at the
end of each chapter serve as a gateway to the growing body of
literature in the field.
With the publication of Protein and Peptide Folding, Misfolding,
and Non-Folding, researchers now have a single place to discover
IDPs, their diverse biological functions, and the many disciplines
that have contributed to our evolving understanding of them.
peptides, including their role in neurodegenerative diseases
With the discovery of intrinsically disordered proteins and
peptides (IDPs), researchers realized that proteins do not
necessarily adopt a well defined secondary and tertiary structure
in order to perform biological functions. In fact, IDPs play
biologically relevant roles, acting as inhibitors, scavengers, and
even facilitating DNA/RNA-protein interactions. Due to their
propensity for self-aggregation and fibril formation, some IDPs are
involved in neurodegenerative diseases such as Parkinson's and
Alzheimer's.
With contributions from leading researchers, this text reviews
the most recent studies, encapsulating our understanding of IDPs.
The authors explain how the growing body of IDP research is
building our knowledge of the folding process, the binding of
ligands to receptor molecules, and peptide self-aggregation.
Readers will discover a variety of experimental, theoretical, and
computational approaches used to better understand the properties
and function of IDPs. Moreover, they'll discover the role of IDPs
in human disease and as drug targets.
Protein and Peptide Folding, Misfolding, and Non-Folding begins
with an introduction that explains why research on IDPs has
significantly expanded in the past few years. Next, the book is
divided into three sections:
* Conformational Analysis of Unfolded States
* Disordered Peptides and Molecular Recognition
* Aggregation of Disordered Peptides
Throughout the book, detailed figures help readers understand
the structure, properties, and function of IDPs. References at the
end of each chapter serve as a gateway to the growing body of
literature in the field.
With the publication of Protein and Peptide Folding, Misfolding,
and Non-Folding, researchers now have a single place to discover
IDPs, their diverse biological functions, and the many disciplines
that have contributed to our evolving understanding of them.
Autoren-Porträt
Reinhard Schweitzer-Stenner, PhD, is Professor and currently the Head of the Chemistry Department at Drexel University. Dr. Schweitzer-Stenner also heads the biospectroscopy research group. His research investigates peptide structure and functionally relevant heme distortions as well as ligand-receptor binding on the surface of mast cells. With more than 150 published research articles, Dr. Schweitzer-Stenner is widely recognized as a leader and pioneer in the study of the conformational properties of unfolded peptides.
Bibliographische Angaben
- 2012, 1. Auflage, 576 Seiten, Englisch
- Herausgegeben: Reinhard Schweitzer-Stenner
- Verlag: John Wiley & Sons
- ISBN-10: 1118183355
- ISBN-13: 9781118183359
- Erscheinungsdatum: 08.02.2012
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- Größe: 14 MB
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Sprache:
Englisch
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