The impact of conformational fluctuations on self-assembly: cooperative aggregation of archaeal chaperonin proteins.

Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions

Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...

Determination of mercury (II) by spectrophotometric method based on self assembly of gold nanoparticles

Due to the binding of the –COO- group with the mercury (II), gold nanoparticlesfunctionalized with glutathione can self-assemble to form a supermolecular network in the HAc-NaAc buffer solution. The aggregation of functionalized gold nanoparticles and mercury (II)caused the shift of maximum absorption peak of the UV-Vis spectrum from 520 nm to 609 nm.Based on this principle, a simple spectropho...

Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin AUTHORS

Recurrent paralogy in the evolution of archaeal chaperonins

Chaperonins are multisubunit double-ring complexes that mediate the folding of nascent proteins [1] [2]. In bacteria, chaperonins are homo-oligomeric and are composed of seven-membered rings. Eukaryotic and most archaeal chaperonin rings are eight-membered and exhibit varying degrees of hetero-oligomerism [3] [4]. We have cloned and sequenced seven new genes encoding chaperonin subunits from th...

Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis.

We report the characterization of the first chaperonin (Mm-cpn) from a mesophilic archaeon, Methanococcus maripaludis. The single gene was cloned from genomic DNA and expressed in Escherichia coli to produce a recombinant protein of 543 amino acids. In contrast with other known archaeal chaperonins, Mm-cpn is fully functional in all respects under physiological conditions of 37 degrees C. The c...