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Conformation of Biopolymers: Papers Read at an International Symposium Held at the University of Madras, 18-21 January 1967
Conformation of Biopolymers: Papers Read at an International Symposium Held at the University of Madras, 18-21 January 1967
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285 pages
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Conformation of Biopolymers, Volume 2 provides information pertinent to proteins, polypeptides, and polysaccharides. This book discusses the development in the studies on collagen and related polypeptides.
Organized into three parts encompassing 24 chapters, this volume begins with an overview of the structure of polyglycine II with chains running in opposite directions as indicated by the existence of lamellar crystals in electron microscopy. This text then explores the capability of various polypeptides to form the collagen fold. Other chapters consider the effect of pyrrolidine residues on the helix–coil transitions of different native collagens and cross-linked single chain gelatins. This book discusses as well the results of hydrodynamic experiments on native amylose. The final chapter deals with X-ray and electron microscope studies, which are described for two principal types of chitin–protein complex found in insect cuticles.
This book is a valuable resource for physicists, biophysicists, crystallographers, and research workers.
Organized into three parts encompassing 24 chapters, this volume begins with an overview of the structure of polyglycine II with chains running in opposite directions as indicated by the existence of lamellar crystals in electron microscopy. This text then explores the capability of various polypeptides to form the collagen fold. Other chapters consider the effect of pyrrolidine residues on the helix–coil transitions of different native collagens and cross-linked single chain gelatins. This book discusses as well the results of hydrodynamic experiments on native amylose. The final chapter deals with X-ray and electron microscope studies, which are described for two principal types of chitin–protein complex found in insect cuticles.
This book is a valuable resource for physicists, biophysicists, crystallographers, and research workers.
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