Overview
- Editors:
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John J. Kasianowicz
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Biotechnology Division, National Institute of Standards and Technology, Gaithersburg, USA
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Miklós S. Z. Kellermayer
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Department of Biophysics, Pécs University Medical School, Pécs, Hungary
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David W. Deamer
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Biophysics Laboratory, Department of Chemistry and Biochemistry, University of California, Santa Cruz, USA
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Table of contents (23 papers)
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- Zeno Farkas, Imre Derényi, Tomas Vicsek
Pages 327-332
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- Alexei R. Khokhlov, Victor A. Ivanov, Alexander V. Chertovich, Alexei A. Lazutin, Pavel G. Khalatur
Pages 333-350
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- Peter M. Goodwin, W. Patrick Ambrose, Hong Cai, W. Kevin Grace, Erica J. Larson, Babetta L. Marrone et al.
Pages 351-370
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Back Matter
Pages 385-390
About this book
Polymers are essential to biology because they can have enough stable degrees of freedom to store the molecular code of heredity and to express the sequences needed to manufacture new molecules. Through these they perform or control virtually every function in life. Although some biopolymers are created and spend their entire career in the relatively large free space inside cells or organelles, many biopolymers must migrate through a narrow passageway to get to their targeted destination. This suggests the questions: How does confining a polymer affect its behavior and function? What does that tell us about the interactions between the monomers that comprise the polymer and the molecules that confine it? Can we design and build devices that mimic the functions of these nanoscale systems? The NATO Advanced Research Workshop brought together for four days in Bikal, Hungary over forty experts in experimental and theoretical biophysics, molecular biology, biophysical chemistry, and biochemistry interested in these questions. Their papers collected in this book provide insight on biological processes involving confinement and form a basis for new biotechnological applications using polymers. In his paper Edmund DiMarzio asks: What is so special about polymers? Why are polymers so prevalent in living things? The chemist says the reason is that a protein made of N amino acids can have any of 20 different kinds at each position along the chain, resulting in 20 N different polymers, and that the complexity of life lies in this variety.
Editors and Affiliations
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Biotechnology Division, National Institute of Standards and Technology, Gaithersburg, USA
John J. Kasianowicz
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Department of Biophysics, Pécs University Medical School, Pécs, Hungary
Miklós S. Z. Kellermayer
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Biophysics Laboratory, Department of Chemistry and Biochemistry, University of California, Santa Cruz, USA
David W. Deamer