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Alpha -lactalbumin
Small acidic protein a-lactalbumin, one of the major protein components of milk, is one of the most extensively investigated Ca2+-binding proteins, which does not belong to the EF-hand family of calcium-binding proteins. It serves as a model for studies of the mechanisms of protein stability, folding and unfolding. a-Lactalbumin acts as a regulatory subunit of galactosyltransferase in lactose synthase, which catalyses the synthesis of lactose from UDP-galactose and glucose. It represents a classical example of molten globule state at acidic pH and in its apo-form at elevated temperatures. Three-dimensional structures of several ?-lactalbumins are determined. The protein possesses a single st...
Methods in Protein Structure and Stability Analysis: Conformational stability, size, shape, and surface of protein molecules
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.
Methods in Protein Structure and Stability Analysis: Vibrational spectroscopy
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.
Ribonucleotide Reductase
The subject of this book is the amazing enzyme ribonucleotide reductase (RNR), the enzyme responsible for the conversion of ribonucleotides to deoxyribonucleotides. The prerequisite for DNA-synthesis and DNA-repair in all living cells is the supply of the four deoxyribonucleotides. Such molecules result from the enzymatically difficult radical-induced reduction of ribonucleotides, a multistep chemical process catalyzed by RNR. RNR was the first enzyme in which the presence of an amino acid radical (a tyrosyl) in E. coli Class Ia RNR has been proven; since then several other biological amino acid radical species have been found on e.g. tryptophan, glycine, cysteine, lysine residues and on amino acid derived small cofactors like 2 tryptophanes in thryptophan-trypthanyl-radical or cysteine-tyrosyl-radical in other enzymes. As all known cellular life forms store their genetic information as DNA, RNR is likely to be found in all growing cells of every living organism, a fact that is confirmed by a rapidly increasing number of genomic screenings.
Parvalbumin
Parvalbumin is a small (Mr 12,000), acidic (pI 4-5), Ca2+-binding protein of the EF-hand superfamily, that is very important from several points of view. First of all, this protein takes part in Ca2+ regulation of activity of some types of muscle cells, neurons and some other types of cells. At the same time, the exact physiological role of parvalbumin in some of these cells is not clear enough now. Second, parvalbumin has two high affinity Ca2+ binding sites and for this reason it is frequently used as a simple model Ca2+ binding protein. It is convenient for studies of effects of interactions between two calcium binding sites and is very useful for studies of calcium binding effects on int...
Instrumental Analysis of Intrinsically Disordered Proteins
Instrumental techniques for analyzing intrinsically disordered proteins The recently recognized phenomenon of protein intrinsic disorder is gaining significant interest among researchers, especially as the number of proteins and protein domains that have been shown to be intrinsically disordered rapidly grows. The first reference to tackle this little-documented area, Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation provides researchers with a much-needed, comprehensive summary of recent achievements in the methods for structural characterization of intrinsically disordered proteins (IDPs). Chapters discuss: Assessment of IDPs in the living cel...
Current Catalog
First multi-year cumulation covers six years: 1965-70.
Unfolded Proteins
The word revolution has a number of definitions (The American Heritage Dictionary, 2006). The one most pertinent to this series and volume is 'a sudden or momentous change in a situation'. Recent years have seen an unprecedented explosion of interest in unfolded proteins in all of their various forms. Coupled with this increase in interest we have seen momentous changes in the way unfolded proteins are viewed. Two particular paradigms have come under close scrutiny: unfolded proteins are disordered random coils devoid of persistent structure, and protein function first requires protein structure. The first of these is currently a hotly debated subject. The second paradigm we can safely claim...
