Toshio Ando – författare

A century has already passed since FRIEDRICH MIESCHER, working at Strasbourg and Basel, began his study of protamine, one of the basic nuclear proteins of cells. It was first established by KOSSEL that protamine represents the simplest known protein. In the conviction that research into the nature of protamine would shed light on that of other typical proteins, a group of researchers in Germany followed MIESCHER and laid the foundations of protein chemistry. A general view of prot­ amines was thus built up by KOSSEL, working at Strasbourg, Berlin, Marburg an der Lahn, and Heidelberg, FELIX at Heidelberg, Munich, and Frankfurt am Main, and WALDSCHMIDT-LEITZ at Prague and Munich. Concepts and techniques established by these studies have been widely utilized for research on other typical proteins. The revolutionary advances in chemical and physical techniques after W orId War II extended the sphere of research to Tokyo in the Far East. Prof. FELIX'' visit in 1955 greatly encouraged our research group in Tokyo. His death in August 1960 constituted a sad loss to protein chemistry and stimulated our group to assume responsibility for carrying on the studies. In the following decade we in Tokyo have been able to add a new development to the results on the chemical structure of protamines accumulated by the Eurqpean researchers over a period of about fifty years.

A century has already passed since FRIEDRICH MIESCHER, working at Strasbourg and Basel, began his study of protamine, one of the basic nuclear proteins of cells. It was first established by KOSSEL that protamine represents the simplest known protein. In the conviction that research into the nature of protamine would shed light on that of other typical proteins, a group of researchers in Germany followed MIESCHER and laid the foundations of protein chemistry. A general view of prot­ amines was thus built up by KOSSEL, working at Strasbourg, Berlin, Marburg an der Lahn, and Heidelberg, FELIX at Heidelberg, Munich, and Frankfurt am Main, and WALDSCHMIDT-LEITZ at Prague and Munich. Concepts and techniques established by these studies have been widely utilized for research on other typical proteins. The revolutionary advances in chemical and physical techniques after W orId War II extended the sphere of research to Tokyo in the Far East. Prof. FELIX' visit in 1955 greatly encouraged our research group in Tokyo. His death in August 1960 constituted a sad loss to protein chemistry and stimulated our group to assume responsibility for carrying on the studies. In the following decade we in Tokyo have been able to add a new development to the results on the chemical structure of protamines accumulated by the Eurqpean researchers over a period of about fifty years.

This first book on high-speed atomic force microscopy (HS-AFM) is intended for students and biologists who want to use HS-AFM in their research. It provides straightforward explanations of the principle and techniques of AFM and HS-AFM. Numerous examples of HS-AFM studies on proteins demonstrate how to apply this new form of microscopy to specific biological problems. Several precautions for successful imaging and the preparation of cantilever tips and substrate surfaces will greatly benefit first-time users of HS-AFM. In turn, the instrumentation techniques detailed in Chapter 4 can be skipped, but will be useful for engineers and scientists who want to develop the next generation of high-speed scanning probe microscopes for biology.The book is intended to facilitate the first-time use of this new technique, and to inspire students and researchers to tackle their own specific biological problems by directly observing dynamic events occurring in the nanoscopic world. Microscopy in biology has recently entered a new era with the advent of high-speed atomic force microscopy (HS-AFM). Unlike optical microscopy, electron microscopy, and conventional slow AFM, it allows us to directly observe biological molecules in physiological environments. Molecular “movies” created using HS-AFM can directly reveal how molecules behave and operate, without the need for subsequent complex analyses and roundabout interpretations. It also allows us to directly monitor morphological change in live cells, and dynamic molecular events occurring on the surfaces of living bacteria and intracellular organelles. As HS-AFM instruments were recently commercialized, in the near future HS-AFM is expected to become a common tool in biology, and will enhance and accelerate our understanding of biological phenomena.