Transfer molding of PMR-15 polyimide resin

Transfer molding is an economically viable method of producing small shapes of PMR-15 polyimide. It is shown that with regard to flexural, compressive, and tribological properties transfer-molded PMR-15 polyimide is essentially equivalent to PMR-15 polyimide produced by the more common method of compression molding. Minor variations in anisotropy are predictable effects of molding design and secondary finishing operations

DETERMINANTS OF FERTILIZER ADOPTION BY AFRICAN FARMERS: POLICY ANALYSIS FRAMEWORK, ILLUSTRATIVE EVIDENCE, AND IMPLICATIONS

Crop Production/Industries,

Improving the Measurement and Analysis of African Agricultural Productivity: Promoting Complementarities between Micro and Macro Data

Productivity Analysis,

Promoting Farm Investment for Sustainable Intensification of African Agriculture

Farm Management, Downloads July 2008-July 2009: 9,

Cash Crop and Foodgrain Productivity in Senegal: Historical View, New Survey Evidence, and Policy Implications

Crop Production/Industries, Productivity Analysis, Downloads July 2008 - June 2009: 10,

Approximate analysis and stability of pressure oscillations in ramjets

This paper summarizes work accomplished during the past five years on analysis of stability related to recent experimental results on combustion instabilities in dump combustors. The primary purpose is to provide the information in a form useful to those concerned with design and development of operational systems. Thus most substantial details are omitted; the material is presented in a qualitative fashion

Analysis of existing mathematics textbooks for use in secondary schools.

Thesis (Ed.M.)--Boston University Thesis (M.A.)--Boston Universit

Calorimetric Analysis Using DNA Thermal Stability to determine protein concentration

It was recently reported for two globular proteins and a short DNA hairpin in NaCl buffer that values of the transition heat capacities, Cp,DNA and Cp,PRO for equal concentrations (mg/mL) of DNA and proteins, are essentially equivalent (differ by less than 1%). Additional evidence for this equivalence is presented that reveals this phenomenon does not depend on DNA sequence, buffer salt, or Tm. Sequences of two DNA hairpins were designed to confer a near 20°C difference in their Tm’s. For the molecules, in NaCl and CsCl buffer the evaluated Cp,PRO and Cp,DNA were equivalent. Based on the equivalence of transition heat capacities, a calorimetric method was devised to determine protein concentrations in pure and complex solutions. The scheme uses direct comparisons between the thermodynamic stability of a short DNA hairpin standard of known concentration, and thermodynamic stability of protein solutions of unknown concentrations. In all cases, evaluated protein concentrations determined from the DNA standard curve agreed with the UV-Vis concentration for monomeric proteins. For samples of multimeric proteins, streptavidin (tetramer), Herpes Simplex Virus glycoprotein D (trimer/dimer), and a 16 base pair DNA duplex (dimer), evaluated concentrations were greater than determined by UV-Vis by factors of 3.94, 2.65, and 2.15, respectively

DNA-based Assay for Calorimetric determination of protein concentrations in pure or mixed solutions

It was recently reported that values of the transition heat capacities, as measured by differential scanning calorimetry, for two globular proteins and a short DNA hairpin in NaCl buffer are essentially equivalent, at equal concentrations (mg/mL). To validate the broad applicability of this phenomenon, additional evidence for this equivalence is presented that reveals it does not depend on DNA sequence, buffer salt, or transition temperature (Tm). Based on the equivalence of transition heat capacities, a calorimetric method was devised to determine protein concentrations in pure and complex solutions. The scheme uses direct comparisons between the thermodynamic stability of a short DNA hairpin standard of known concentration, and thermodynamic stability of protein solutions of unknown concentrations. Sequences of two DNA hairpins were designed to confer a near 20˚C difference in their Tm values. In all cases, evaluated protein concentrations determined from the DNA standard curves agreed with the UV-Vis concentration for monomeric proteins. For multimeric proteins evaluated concentrations were greater than determined by UV-Vis suggesting the calorimetric approach can also be an indicator of molecular stoichiometry