Asylum Research will sponsor a free atomic force microscopy (AFM) Workshop on February 12 and 13, 2009 in the Pettit Building/Microelectronics Research Center (MiRC) on the Georgia Institute of Technology campus.
A new open-source software package developed at Stanford University is making it possible to do complex simulations of molecular motion on desktop computers at much faster speeds than has been previously possible.
From mid-February 2009, EthicSchool distributes 500 e-learning DVDs on Ethics of Nanotechnology and of Converging Technologies for free to lecturers giving courses on Ethics of Science and Technology, and for self-study.
The project, called 'Engineered Nanoparticles: Review of Health and Environmental Safety (ENRHES)', involves a survey to gather information from manufacturers and uses of nanomaterials to provide context for the scientific review and inform the risk assessment considerations.
An international team of scientists led by the University of Leeds has shed new light on the little-understood motor protein called dynein, thought to be involved in progressive neurological disorders such as motor neurone disease.
Scientists at the Naval Research Laboratory (NRL) have recently demonstrated the ability to control the spin population of the individual quantum shell states of self-assembled indium arsenide (InAs) quantum dots.
University of Utah physicists and chemists developed a new method that uses a mirror of tiny silver nanoparticles so microscopes can reveal the internal structure of nearly opaque biological materials like bone or tumor cells.
The National Nanotechnology Coordination Office, on behalf of the NSET Subcommittee, will hold a February 24-25, 2009 workshop to provide an open forum to discuss the state-of-the-art of the science related to environmental, health, and safety aspects of engineered nanoscale materials in the area of Human and Environmental Exposure Assessment.
MIT researchers who study the structure of protein-based materials with the aim of learning the key to their lightweight and robust strength have discovered that the particular arrangement of proteins that produces the sturdiest product is not the arrangement with the most built-in redundancy or the most complicated pattern.