Identification of phenological stages and vegetative types for land use classification

There are no author-identified significant results in this report

Spectrin promotes the association of F-actin with the cytoplasmic surface of the human erythrocyte membrane

We studied the binding of actin to the erythrocyte membrane by a novel application of falling ball viscometry. Our approach is based on the notion that if membranes have multiple binding sites for F-actin they will be able to cross-link and increase the viscosity of actin. Spectrin- and actin-depleted inside-out vesicles reconstituted with purified spectrin dimer or tetramer induce large increases in the viscosity of actin. Comparable concentrations of spectrin alone, inside-out vesicles alone, inside-out vesicles plus heat-denatured spectrin dimmer or tetramer induce large increases in the viscosity of actin. Comparable concentrations of spectrin alone, inside-out vesicles alone, inside-out plus heat denatured spectrin, ghosts, or ghosts plus spectrin have no effect on the viscosity of actin. Centrifugation experiments show that the amount of actin bound to the inside-out vesicles is enhanced in the presence of spectrin. The interactions detected by low-shear viscometry reflect actin interaction with membrane- bound spectrin because (a) prior removal of band 4.1 and ankyrin (band 2.1, the high- affinity membrane attachment site for spectrin) reduces both spectrin binding to the inside-out vesicles and their capacity to stimulate increase in viscosity of actin in the presence of spectrin + actin are inhibited by the addition of the water-soluble 72,000- dalton fragment of ankyrin, which is known to inhibit spectrin reassociation to the membrane. The increases in viscosity of actin induced by inside-out vesicles reconstituted with purified spectrin dimer or tetramer are not observed when samples are incubated at 0 degrees C. This temperature dependence may be related to the temperature-dependent associations we observe in solution studies with purified proteins: addition of ankyrin inhibits actin cross-linking by spectrin tetramer plus band 4.1 at 0 degrees C, and enhances it at 32 degrees C. We conclude (a) that falling ball viscometry can be used to assay actin binding to membranes and (b) that spectrin is involved in attaching actin filaments or oligomers to the cytoplasmic surface of the erythrocyte membrane

Design of Low Cost Modular Robotic Manipulator Joints

The goal of this project was to design and manufacture robotic joints that are inexpensive and capable of being used in a variety of applications. In order to maximize the number of applications in which our design could be utilized, research was done on optimal strength, size, communications, modularity, and price. This project includes the research and design development necessary to engineer such a joint, including part selection, motor control, manufacturing processes, and strength analysis. Two Joints were constructed and tested: a rotator joint and a elbow-joint. The joints performed well under testing conditions and overall prices were kept low. With future development, these joints could be used in fields where size and price are critical

EDUCATION AND PRODUCTION Effect of Differing Light Intensities on Abdominal Fat Deposition in Broilers

ABSTRACT Two trials were conducted in an attempt to determine if light intensity affected fat content of broilers as measured by the amount of abdominal fat. The light regimens used from 10 days of age had constant intensities of 2 or 52 lx. Results obtained showed that light intensity did not significantly influence the amount of abdominal fat produced by males or females at either 49 or 63 days of age. Light intensity had no significant effect on body weight, feed conversion (grams feed per gram body weight), or mortality at either 48 or 62 days of age for broilers of the same sex. The amount of light used was the amount produced from either 7.5 or 75-W incandescent bulbs in an enclosed house that was 11m wide with two strings of light bulbs 2.1 m high on 3-m centers equidistant from the ends and sidewalls of the house

Unzipping Kinetics of Double-Stranded DNA in a Nanopore

We studied the unzipping kinetics of single molecules of double-stranded DNA by pulling one of their two strands through a narrow protein pore. PCR analysis yielded the first direct proof of DNA unzipping in such a system. The time to unzip each molecule was inferred from the ionic current signature of DNA traversal. The distribution of times to unzip under various experimental conditions fit a simple kinetic model. Using this model, we estimated the enthalpy barriers to unzipping and the effective charge of a nucleotide in the pore, which was considerably smaller than previously assumed.Comment: 10 pages, 5 figures, Accepted: Physics Review Letter