Indian Institute of Technology Guwahati

About: Indian Institute of Technology Guwahati is a education organization based out in Guwahati, Assam, India. It is known for research contribution in the topics: Catalysis & Computer science. The organization has 6933 authors who have published 17102 publications receiving 257351 citations.

Urban Quality of Life: A Case Study of Guwahati

Abstract: This paper studies quality of life (QOL) in urban environment. The term environment has been used in broader sense, which includes physical, social and economic environment. A framework has been proposed which posits that QOL comprises objective condition of living and satisfaction from such living condition constitutes QOL. Such objective condition refers to objective QOL and satisfaction refers to subjective QOL. Dimension of QOL has been found to be multi dimensional. It has been found that both objective and subjective condition is important dimension of QOL. But correlation between objective and subjective QOL has been found not to be high. At the same time it has been found that satisfaction from condition of traffic is the lowest among all satisfaction variables.

Lysozyme: a model protein for amyloid research.

Abstract: Ever since lysozyme was discovered by Fleming in 1922, this protein has emerged as a model for investigations on protein structure and function. Over the years, several high-resolution structures have yielded a wealth of structural data on this protein. Extensive studies on folding of lysozyme have shown how different regions of this protein dynamically interact with one another. Data is also available from numerous biotechnological studies wherein lysozyme has been employed as a model protein for recovering active recombinant protein from inclusion bodies using small molecules like l-arginine. A variety of conditions have been developed in vitro to induce fibrillation in hen lysozyme. They include (a) acidic pH at elevated temperature, (b) concentrated solutions of ethanol, (c) moderate concentrations of guanidinium hydrochloride at moderate temperature, and (d) alkaline pH at room temperature. This review aims to bring together similarities and differences in aggregation mechanisms, morphology of aggregates, and related issues that arise using the different conditions mentioned above to improve our understanding. The alkaline pH condition (pH 12.2), discovered and studied extensively in our lab, shall receive special attention. More than a decade ago, it was revealed that mutations in human lysozyme can cause accumulation of large quantities of amyloid in liver, kidney, and other regions of gastrointestinal tract. Understanding the mechanism of lysozyme aggregation will probably have therapeutic implications for the treatment of systemic nonneuropathic amyloidosis. Numerous studies have begun to focus attention on inhibition of lysozyme aggregation using antibody or small molecules. The enzymatic activity of lysozyme presents a convenient handle to quantify the native population of lysozyme in a sample where aggregation has been inhibited. The rich information available on lysozyme coupled with the multiple conditions that have been successful in inducing/inhibiting its aggregation in vitro makes lysozyme an ideal model protein to investigate amyloidogenesis.