Published January 1, 1995
by Taylor & Francis .
Written in English
|The Physical Object|
This book serves as an introduction to protein structure and function. Starting with their makeup from simple building blocks, called amino acids, the 3-dimensional structure of proteins is explained. This leads to a discussion how misfolding of proteins causes diseases like cancer, various encephalopathies, or Brand: Springer International Publishing. This book serves as an introduction to protein structure and function. Starting with their makeup from simple building blocks, called amino acids, the 3-dimensional structure of proteins is explained. This leads to a discussion of how misfolding of proteins causes diseases like cancer, various encephalopathies, or diabetes. Protein Physics, Second Edition. A Course of Lectures by Alexei V. Finkelstein and Oleg B. Ptitsyn. Fully revised and updated comprehensive reference providing the fundamental physics behind. Emphasizing concepts and theory rather than experimental techniques, the book shows how proteins can be analyzed using the disciplines of elementary statistical mechanics, energetics, and kinetics. These chapters illuminate how proteins attain biologically active states and the properties of those states.
Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states. The sequence of amino acids determines each protein's unique 3-dimensional structure and its specific function such as catalysis of biochemical reactions, mechanical support and immune protection. While most textbooks on bioinformatics focus on genetic algorithms and treat protein structure prediction only superficially, this course book assumes a novel and unique focus. Adopting a didactic approach, the author explains all the current methods in terms of their reliability, limitations and user-friendliness. She provides practical examples to help first-time users become familiar with. The sequence of the atoms in the polypeptide backbone varies between different proteins. Nonpolar amino acids tend to be found in the interior of proteins. Protein folding can be studied using a solution of purified protein and a denaturant (urea), a solvent that interferes with noncovalent interactions.
These are highlighted as key questions in a nice readable review in Science The Protein Folding problem, 50 years on by Ken Dill and Justin MacCallum. The article gives a sober assessment of limited but significant achievements and the substantial challenges ahead. the globular proteins, function as enzymes, transport proteins, or antibodies. Fibrous proteins tend to be water-insoluble, while globular proteins tend to be water-soluble. Polypeptides are unique among biological molecules in their flex-ibility, which allows them to fold into characteristic three-dimensional. ^ Free Book Protein Folding Kinetics Biophysical Methods ^ Uploaded By Jin Yong, protein folding kinetics biophysical methods is written for students and researchers in biochemistry biophysics and related fields special features in the second edition o includes detailed information and 12 color figures on the high resolution of folding. Proteins: Structure and Function is a comprehensive introduction to the study of proteins and their importance to modern biochemistry. Each chapter addresses the structure and function of proteins with a definitive theme designed to enhance student understanding. Opening with a brief historical overview of the subject the book moves on to discuss the ‘building blocks’ of proteins and their.