Diminishing protein aggregation by chaperone is very important factor in medicine and industry. In this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by Woodward reagentK(WRK) and examined on lysozyme as a target protein at pH 7.2 and outlined the mechanism for chaperoneability of modified system by UV-Vis and fluorescence spectroscopy and theor...

Protein aggregation and precipitation is associated with many debilitating diseases including Alzheimer's, Parkinson's, and light-chain amyloidosis. β-Casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. Hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stab...

diminishing protein aggregation by chaperone is very important factor in medicine and industry. in this paper, itis induced the chaperone ability for 0-casein upon modification of its acidic residues by woodward reagentk(wrk) and examined on lysozyme as a target protein at ph 7.2 and outlined the mechanism for chaperoneability of modified system by uv-vis and fluorescence spectroscopy and theor...

Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was to establish the correlation of structure and function of recombinant Acr proteins both before and after ge...

protein aggregation and precipitation is associated with many debilitating diseases including alzheimer's, parkinson's, and light-chain amyloidosis. β-casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stab...

Nerve growth factor (NGF) is a neurotrophic factor that is functional in the survival, maintenance and differentiation of nervous system cells. This protein has three subunits, of which the beta subunit has the main activity. Its structure consists of a cysteine knot motif made up of beta strands linked by disulfide bonds. It can be used as a therapeutic agent in the treatment of many diseases....

In lysosomal diseases, enzyme deficiency is caused by misfolding of mutant protein with abnormal steric structure that expressed gene mutation. Chaperone therapy a new molecular therapeutic approach primarily for diseases. The misfolded digested rapidly or aggregated to induce endoplasmic reticulum stress. As result, the catalytic activity lost. following sequence events results in chaperone ac...

Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. On the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into Escherichia coli along with human basic Fibroblast Grow...

lysozyme is a bactericidal enzyme whose structure and functions change in diabetes. chemical chaperones are small molecules including polyamines (e.g. spermine), amino acids (e.g. l-lysine) and polyols (e.g. glycerol). they can improve protein conformation in several stressful conditions such as glycation. in this study, the authors aimed to observe the effect of l-lysine as a chemical chaperon...

Single-molecule force spectroscopy provides access to the mechanics of biomolecules. Recently, magnetic and laser optical tweezers were applied in studies chaperones their interaction with protein clients. Various aspects chaperone–client interactions can be revealed based on mechanical probing strategies. First, when a chaperone is probed under load, one examine inner workings while it interac...