....................................................................................................................................1 1. Computational studies of protein folding and aggregation ..........................................3 1.1 Overview ....................................................................................................................3 1.2 Protein structure..........

Aging is the most important risk factor for neurodegenerative diseases associated with pathological protein aggregation such as Alzheimer's disease. Although aging is an important player, it remains unknown which molecular changes are relevant for disease initiation. Recently, it has become apparent that widespread protein aggregation is a common feature of aging. Indeed, several studies demons...

Low molecular size additives such as L-arginine and the redox compounds have been used both in the culturemedium and in vitro refolding to increase recombinant proteins production. Additives increase proteinrefolding and yield of active proteins by suppressing aggregate formation or enhancing refolding process.In this work, a comparative study was performed on refolding of rec...

Protein aggregation is broadly important in diseases and in formulations of biological drugs. Here, we develop a theoretical model for reversible protein-protein aggregation in salt solutions. We treat proteins as hard spheres having square-well-energy binding sites, using Wertheim's thermodynamic perturbation theory. The necessary condition required for such modeling to be realistic is that pr...

Protein aggregation and amyloid formation is a hallmark of an increasing number of human disorders. Because protein aggregation is deleterious for the cell physiology and results in a decrease in overall cell fitness, it is thought that natural selection acts to purify aggregating proteins during evolution. This data article contains complementary figures and results related to the research art...

Polyglutamine (polyQ) diseases are inherited neurodegenerative disorders caused by the expansion of CAG codon repeats, which code for polyQ in the corresponding gene products. These diseases are associated with the presence of amyloid-like protein aggregates, induced by polyQ expansion. It has been suggested that the soluble aggregates rather than the mature fibrillar aggregates are the toxic s...

CD43 (leukosialin, sialophorin), a prominent component of the hemopoietic cell surface, has an enigmatic role in cell-cell interaction. The observation that CD43 ligation triggers homotypic aggregation of monoblastoid U937 cells has permitted analysis of this: CD43-induced aggregation was distinguishable from CD29- (also known as beta1 integrin) or CD98- (also known as 4F2, or fusion-related pr...

Many neurodegenerative disorders like Alzheimer’s, Parkinson’s, prion and polyglutamine diseases are caused by gain-of-function mechanisms in which the disease-causing protein accumulates in the form of insoluble protein aggregates or inclusion bodies [1,2]. Whether these aggregated proteins directly cause neurodegeneration is still controversial; however, it is widely believed that soluble for...

Aggregation (‘‘clumping together’’) of certain cellular proteins is a common feature of a variety of diseases including neurodegenerative conditions such as Parkinson’s, Alzheimer’s, and Huntington’s diseases. Many of these conditions are more prevalent in old age, but the changes that cause increased aggregation of these disease proteins are not well understood. A new study by Cynthia Kenyon a...

Ram Vanam M.S., Indiana University, December 2004. Electrostatic modeling of protein aggregation. Research Advisor: Paul L. Dubin Electrostatic modeling was done with Delphi of insight II to explain and predict protein aggregation, measured here for β-lactoglobulin and insulin using turbidimetry and stopped flow spectrophotometry. The initial rate of aggregation of β-Lactoglobulin was studied b...