The original publication is available through http://www.informaworld.com or directly from the DOI 10.1080/0897719070167977G.
Many proteins, including several growth factor receptors such as the IGF-1R and EGFR family, contain variants of the 
-helix fold. Inspection of the irregular protein -helices suggested that different families of regular -helical
polypeptides can be designed using a series of hinged vectors and the
constraints imposed by the geometry of a peptide backbone. We have
conceived -helices with five and six -strands per turn and designed, in detail, a series of regular -helices with rhomboidal or triangular cross-sections. Each -helix was modeled by threading C
atoms to follow the vectorial -helix
and then creating the H-bonded polypeptide backbone and appropriate
side-chain orientations. The conformational stability of these regular -helices
was assessed using molecular dynamics simulations. Several potential
repeat amino acid sequences were identified for different geometries of
-helix. Regular -helices
offer new possibilities for the study of protein folding, the
production of nanofibers, catalysts, inhibitors of growth factor
receptors and drug carriers.
-helix fold. Inspection of the irregular protein -helices suggested that different families of regular -helical
polypeptides can be designed using a series of hinged vectors and the
constraints imposed by the geometry of a peptide backbone. We have
conceived -helices with five and six -strands per turn and designed, in detail, a series of regular -helices with rhomboidal or triangular cross-sections. Each -helix was modeled by threading C atoms to follow the vectorial -helix
and then creating the H-bonded polypeptide backbone and appropriate
side-chain orientations. The conformational stability of these regular -helices
was assessed using molecular dynamics simulations. Several potential
repeat amino acid sequences were identified for different geometries of
-helix. Regular -helices
offer new possibilities for the study of protein folding, the
production of nanofibers, catalysts, inhibitors of growth factor
receptors and drug carriers.[ bib | .pdf ]
This paper describes current progress of a project, which uses naive physics to enable a robot to perform efficient odor localization. Odor localization is the problem of finding the source of an odor or other volatile chemical. Most localization methods require the robot to follow the odor plume along its entire length, which is time consuming and may be especially difficult in a cluttered environment. These drawbacks are significant in light of potential applications such as search and rescue operations in damaged buildings. In this project a map of the robot?s environment was used, together with a naive physics model of airflow, to predict the pattern of air movement. The robot then used the airflow pattern to reason about the probable location of the odor source. This approach, based on naive physics, has successfully located odor sources in a simplified environment. This demonstrates that naive physics can be used to assist odor localization operations and indicates that similar techniques have great potential for allowing a robot operating in an unstructured environment to reason about its surroundings. This paper presents details of the naive physical model of airflow, the reasoning system, the experimental equipment, and results of practical odor source localization experiments.