Includes bibliographical references and indexes.
|Statement||edited by David A.D. Parry, John M. Squire.|
|Series||Advances in protein chemistry -- v. 70|
|Contributions||Parry, David A. D., Squire, John, 1945-|
|The Physical Object|
|Pagination||xii, 525 p.,  p. of plates :|
|Number of Pages||525|
This book provides the readers with an up-to-date review of the design, structure and function of a representative selection of fibrous proteins in both health and disease. The importance of the α-helical coiled coil, a conformational motif based on the heptad repeat in the amino acid sequence of all α-fibrous proteins (and parts of some globular proteins) is underlined by. Established researchers and postgraduate students in the fields of protein chemistry, biochemistry and structural biophysics will find Fibrous Proteins: Structures and Mechanisms to be an invaluable collection of topical reviews that describe the basic advances made in the field of fibrous proteins over the past decade. This book, written by Author: David A.D. Parry. Other articles where Fibrous protein is discussed: protein: The shape of protein molecules: unidimensional structure of the threadlike fibrous proteins; both were recognized many years before the technique of X-ray diffraction was developed. Solutions of fibrous proteins are extremely viscous (i.e., sticky); those of the globular proteins have low viscosity (i.e., they flow easily). The 3D-shape of globular proteins is critical to their function – slight changes can have radical effects – eg in sickle cell anaemia one amino acid change causes a shape change in the molecule that in turns reduces the ability of haemoglobin to bind to oxygen and changes the shape of the whole red blood cell from a biconcave disk to a 5/5.
Molecular Motors and Muscle is the second of a three-part series on Fibrous Proteins. The books are based on a very successful workshop in Alpbach, Austria on the general topic of Fibrous Proteins that gave rise to the award-winning issue of Journal of Structural Biology. There are two major types of protein: Globular proteins which are often enzymes which speed up biochemical reactions and Format: Hardcover. Comprised of 18 chapters divided into three sections, this book opens with a discussion on the theory and technique of X-ray diffraction applicable to the study of conformation in fibrous materials, along with electron diffraction, electron microscopy, optical diffraction, and infrared spectrophotometry. Collagen is the major insoluble fibrous protein in the extracellular matrix and in connective tissue. In fact, it is the single most abundant protein in the animal kingdom. There are at least 16 types of collagen, but 80 – 90 percent of the collagen in the body consists of types I, II, and III (Table ). These collagen molecules pack together to form long thin fibrils of similar structure Cited by: Learn fibrous proteins with free interactive flashcards. Choose from different sets of fibrous proteins flashcards on Quizlet.
Proteins exhibiting these traits are commonly insoluble in water and are referred to as fibrous proteins (also called scleroproteins). The examples described in this category are found exclusively in animals where they serve roles in flesh, connective tissues and hardened external structures, such as hair. The book is aimed for an audience of graduate students and scientists and will provide the opportunity to highlight the field of fibrous proteins. Instructors We provide complimentary e-inspection copies of primary textbooks to instructors considering our books for course adoption. Proteins come in various sizes and shapes. Those with thread-like shapes, the fibrous proteins, tend to have structural or mechanical roles. Those with spherical shapes, the globular proteins, function as enzymes, transport proteins, or antibodies. Fibrous proteins tend to be water-insoluble, while globular proteins tend to be Size: 2MB. Fibrous Proteins will give an overview over some of the most important fibrous proteins including amyloids, collagens, fibrin, flagella, intermediate filaments, microtubules, silks concerning structure and function and possible applications as our knowledge on globular proteins has been increasing over the past decades, fibrillar.