Protein Structural Analysis, Folding and Design

Our understanding of the structure-function relationship in proteins was revolutionized in the 1980's by the use of site-directed mutagenesis coupled with X-ray crystallography, which reveals the story of protein functions in their atomic resolution. This was still limited, however, to the hydrolytic enzymes hemoproteins such as myoglobin and hemoglobin. Our knowledge of protein-functions is also being increased through such computer-aided approaches as graphic design and molecular mechanics, although these approaches too are currently applicable for smaller proteins. From 1986 to 1988 a group of Japanese scientists pursued research on the structural analyses, folding and design of various types of proteins including cytochrome P450, ferredoxins, hemoglobin, erbutoxin, neurotoxins, tryptophan synthase, thermophile isopropylmaleate dehydrogenase, fatty acid synthetase, ion-channel proteins and abnormal hemoglobins. Their findings are summarized in this volume, providing data on the capability and potential of site-directed mutagenesis, mutations in nature, and computer-aided predictions for more complicated proteins.
 
Our understanding of the structure-function relationship in proteins was revolutionized in the 1980's by the use of site-directed mutagenesis coupled with X-ray crystallography, which reveals the story of protein functions in their atomic resolution. This was still limited, however, to the hydrolytic enzymes hemoproteins such as myoglobin and hemoglobin. Our knowledge of protein-functions is also being increased through such computer-aided approaches as graphic design and molecular mechanics, although these approaches too are currently applicable for smaller proteins. From 1986 to 1988 a group of Japanese scientists pursued research on the structural analyses, folding and design of various types of proteins including cytochrome P450, ferredoxins, hemoglobin, erbutoxin, neurotoxins, tryptophan synthase, thermophile isopropylmaleate dehydrogenase, fatty acid synthetase, ion-channel proteins and abnormal hemoglobins. Their findings are summarized in this volume, providing data on the capability and potential of site-directed mutagenesis, mutations in nature, and computer-aided predictions for more complicated proteins.