This first volume provides a comprehensive overview on evolutionary, environmental and systematic aspects of antifreeze proteins. It shortly explains the physical properties of ice and further intelligibly describes the biology of the antifreeze proteins in different organisms, and offers a detailed insight into their history of evolution. In addition the book discusses the status of the current knowledge and ongoing research and highlights also those parts, where further investigation needs to be done. Together with the second volume on the biochemistry and molecular biology of antifreeze proteins, this book represents a unique, comprehensive work and a must-have for students and scientists in biochemistry, evolution, physiology and physical chemistry.
This second volume, written in four parts, offers the reader a thorough review on molecular, structural and applied aspects of antifreeze proteins. The first part treats the structure-function relationship and the physicochemical properties of antifreeze proteins; the second part provides insight into molecular mechanisms affected by antifreeze proteins; the third part presents some of the potential applications in various professional sectors and in the last part the book content is summarized and future research directions and ideas are discussed. Together with the first volume on the environment, systematic and evolution of antifreeze proteins, this book represents a unique, comprehensive work and a must-have for students and scientists in biochemistry, molecular biology, biotechnology and physical chemistry.
In their very first lecture biochemists learn that biomolecules, namely nucleic acids, proteins and lipids, are extremely temperature sensitive and will denature and lose their function easily. Then how do Archaebacteria survive in hot springs or Antarctic fishes which live in ice-cold water? The way nature engineered subcellular structures, lipid membranes or proteins to meet the biochemical requirements of extreme conditions - like extreme temperature or salt concentrations - is described in Life Under Extreme Conditions.
Studies on transgenic fish, in contrast to mammals, are still in their infancy. However, it is evident that such fish will not only be of considerable economic benefit to aquaculture but will enable scientists to make quantum leaps in their understanding of the physiological and biochemical mechanisms unique to fish, and of the developmental biology of vertebrates in general.The potential of transgenic fish for research and industrial development is beginning to be widely recognized. This timely volume encompasses the full spectrum of current research on transgenic fish. It will be valuable to many scientists who intend to explore the merits of the technology for the first time.
Antifreeze proteins, also known as thermal hysteresis proteins, ice binding proteins and ice structuring proteins, prevent the growth of ice crystals in several cold blooded organisms. First discovered in fish, they have also been found in insects, plants, fungi and bacteria. Antifreeze proteins cause the non-colligative depression of the freezing point of water, a property which has been exploited in the practical applications of antifreeze proteins such as improving the texture of ice cream, and could be used to extend the crop growing season or allow fish to thrive in cold waters. This book provides clear information on what is known about antifreeze proteins today and how to study them.
Food proteins and bioactive peptides play a vital role in thegrowth and development of the body’s structural integrity andregulation, as well as having a variety of other functionalproperties. Land animal-derived food proteins such as collagen andgelatine carry risks of contamination (such as BSE). Marine-derivedproteins, which can provide equivalents to collagen and gelatinwithout the associated risks, are becoming more popular amongconsumers because of their numerous health beneficial effects. Mostmarine-derived bioactive peptides are currently underutilized.While fish and shellfish are perhaps the most obvious sources ofsuch proteins and peptides, there is also the potential for furtherdevelopment of proteins and peptides from sources like algae, seacucumber and molluscs. Marine-derived proteins and peptides alsohave potential uses in novel products, with the possibility of widecommercialization in the food, beverage, pharmaceutical andcosmetic industries, as well as in other fields such asphotography, textiles, leather, electronics, medicine andbiotechnology. Marine Proteins and Peptides: Biological Activities andApplications presents an overview of the current status,future industrial perspectives and commercial trends of bioactivemarine-derived proteins and peptides. Many of the industrialperspectives are drawn from the food industry, but the book alsorefers to the pharmaceutical and cosmetics industries. There haverecently been significant advances in isolating functionalingredients from marine bio-resources and seafood by-products foruse in these industries, but little has been published, creating aknowledge gap, particularly with regard to the isolation andpurification processes. This book is the first to fill thatgap. Marine Proteins and Peptides: Biological Activities andApplications is a valuable resource for researchers inmarine biochemistry field as well as food industry managersinterested in exploring novel techniques and knowledge onalternative food protein sources. It will become a standardreference book for researchers involved in developing marinebio-resources and seafood by-products for novel nutraceutical,cosmetics, and pharmaceutical applications. It will also appeal tomanagers and product developers in the food, pharmaceutical andcosmetics industries, particularly those looking to usemarine-derived proteins and peptides as substitutes or replacementsfor unfashionable or outdated food components.
Protein folding is a process by which a protein structure assumes its functional shape of conformation, and has been the subject of research since the publication of the first software tool for protein structure prediction. Protein folding in silico approaches this issue by introducing an ab initio model that attempts to simulate as far as possible the folding process as it takes place in vivo, and attempts to construct a mechanistic model on the basis of the predictions made. The opening chapters discuss the early stage intermediate and late stage intermediate models, followed by a discussion of structural information that affects the interpretation of the folding process. The second half of the book covers a variety of topics including ligand binding site recognition, the "fuzzy oil drop" model and its use in simulation of the polypeptide chain, and misfolded proteins. The book ends with an overview of a number of other ab initio methods for protein structure predictions and some concluding remarks. Discusses a range of ab initio models for protein structure prediction Introduces a unique model based on experimental observations Describes various methods for the quantitative assessment of the presented models from the viewpoint of information theory