Proteins with wholly or partly denatured structure in vivo are called intrinsically disordered or natively unfolded proteins (NUPs). Functional importance of NUPs has been revealed by NMR studies as first reviewed by P. Wright in 1999. Since then, computational analyses on NUPs have also been intensively carried out to predict that about one third of eukaryotic proteins are occupied by NUPs. I will start my overview with a question why it was historically so late to find out NUPs as one of important subjects of protein science, and then move on to several issues such as, whether NUPs are really specific to eukaryotes or not, what means a particularly higher fraction of NUPs existing in the cell nucleus, what is the evolutionary implications of NUPs and so on. The contents will be described from rather a personal point of view.
This paper describes a noble microscope system that can track a swimming microorganism in the center of view field using high-speed visual feedback. The target specimen was tracked by moving its container by a computer controlled XYZ-stage. Target position was extracted from images captured at 1000 fps by a high-speed vision system mounted on the microscope. In this paper, the reason why such high-speed visual feedback is essential for the visual tracking function is discussed. Successful tracking of a freely swimming paramecium and a spermatozoa demonstrated validity of the tracking microscope.