Management of capitalinthe banking system of Ukraine

Дисертація присвячена розвитку існуючих та обґрунтуванню ряду нових науково-методичних та практичних положень упрaвління кaпіталоутворенням в банківській системі (УКБС). В роботі узaгальнено теоретичні дослідження сутності прoцесу капіталоутворення з тoчки зoру абстрaктного та конкрeтного кaпіталу; визнaчено сутність банкіського капіталу у вузькoму (підприємницькoму) знaченні та в ширoкому (суспiльному) знaченні; oбґрунтовано сутнiсть УКБС; визнaчено основні функції БК зaлежно від трaктування його сутнoсті та eтапів життєвoго циклу бaнку; запрoпоновано пiдхід до структуризaції банківського капіталу на основі пoєднання наступних ознaк: підхід до трaктування його сутності, джерела капіталоутворення та можливість упрaвління ними, виходячи з рiвня їх вoлатильності; визначено основні тенденції та виявлено проблеми УКБС України, обґрунтовано шляхи їх вирiшення; здiйснено пoелементне та iнтегральне oцінювання фaкторів впливу на обсяги влaсного капіталу банків України; побудовано мoделі трендів oсновних фaкторів капіталоутворення в банківській системі України за 2007–2012 рр. та cпрогнозовано тeнденції їх змiни на 2014–2016 рр.Dissertation is devoted to the development of existing and new scientific substantiation of a number of methodological and practical provisions of management of capital formation in the banking system, allowing to prove the nature of capital in the banking system, management and conceptual basis of a systematic approach to management of capital formation in the banking system. The paper summarizes theoretical study of the essence of the process of capital formation in terms of abstract and specific capital and the essence of bank capital in the narrow (business) sense and in a wide (public) meaning, an approach to structuring of bank capital based on a combination of the following characteristics : an approach to the interpretation of the essence of bank capital, sources of capital and the ability to manage them based on their level of volatility , by -element and integral evaluation of factors influencing the volume of bank equity capital of Ukraine, the models trending main factors of capital in the banking system Ukraine for 2007–2012 years and predicted trend of changes for 2014–2016 years

Micellization and adsorption characteristics of CHAPS

The adsorption of CHAPS on hydrophobic latex particles was studied at 22 and 36 degrees C by determining the adsorbed amount and the enthalpy of adsorption. The adsorption process was compared to the micellization of the surfactant. Therefore, the critical micelle concentration (cmc) and the heat of micellization were also determined at both temperatures. From these two quantities the Gibbs energy and the entropy of the process were calculated. The cmc and the heat of micellization are temperature dependent; the cmc increases as the temperature rises, and the heat of micellization goes from positive at 22 degrees C to negative at 36 degrees C. There is an entropy-enthalpy compensation in the micellization process, characteristic of hydrophobic interactions. The maximum adsorbed amount is independent of the temperature, while the initial slope of the isotherms is slightly steeper at 22 degrees C. Although the adsorption process is exothermic at both temperatures, the enthalpy of adsorption is more negative at 36 degrees C. Since the adsorption process is more favorable at 22 degrees C, there is a substantial entropy contribution to the overall process, suggesting that hydrophobic interactions are also dominating the adsorption of CHAPS on latex particles. The orientation of the hydroxyl groups in the steroid nucleus of the surfactant is mainly responsible for the aggregation and adsorption behavior of CHAPS. Indeed, the mechanisms of the micellization and the adsorption processes are strongly related: both are driven by hydrophobic interactions between the apolar faces of the CHAPS molecules (micellization) or between the hydrophobic parts of the molecules and the hydrophobic latex particle surface (adsorption)

Engineering antibodies for stability and efficient folding

Antibody variable domains vary widely in their intrinsic thermodynamic stability. Despite the mutual stabilization of the domains in the scFv fragment, most scFv derived from monoclonal antibodies without further engineering show poor to moderate stability. The situation gets more complex for Fab fragments and full-sized antibodies: while the disulfide-linked C(L)/C(H) heterodimer shows very limited thermodynamic stability, its unfolding kinetics are very slow. The same is true for Fab fragments, which, due to this kinetic stabilization, appear to be more stable than their thermodynamic stability suggests. However, suboptimal variable domains can be engineered for improved stability and folding efficiency while preserving their antigen-binding specificity and affinity, either by a limited number of point mutations or by grafting their antigen specificity to superior variable domain frameworks