Search for: protein-multimerization
Article Nanoscale ; Volume 5, Issue 7 , Jan , 2013 , Pages 2570-2588 ; 20403364 (ISSN) ; Kalhor, H. R ; Laurent, S ; Lynch, I ; Sharif University of Technology
Due to their ultra-small size, nanoparticles (NPs) have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. NPs are recognized as promising and powerful tools to fight against the human brain diseases such as multiple sclerosis or Alzheimer's disease. In this review, after an introductory part on the nature of protein fibrillation and the existing approaches for its investigations, the effects of NPs on the fibrillation process have been considered. More specifically, the role of biophysicochemical properties of NPs, which define their affinity for protein monomers, unfolded monomers,...
Article Physical Review E - Statistical, Nonlinear, and Soft Matter Physics ; Volume 93, Issue 1 , 2016 ; 15393755 (ISSN) ; Khoshnood, A ; Jalali, M. A ; Sharif University of Technology
American Physical Society
Protein aggregation in cell membrane is vital for the majority of biological functions. Recent experimental results suggest that transmembrane domains of proteins such as α-helices and β-sheets have different structural rigidities. We use molecular dynamics simulation of a coarse-grained model of protein-embedded lipid membranes to investigate the mechanisms of protein clustering. For a variety of protein concentrations, our simulations under thermal equilibrium conditions reveal that the structural rigidity of transmembrane domains dramatically affects interactions and changes the shape of the cluster. We have observed stable large aggregates even in the absence of hydrophobic mismatch,...
Article Journal of Biomechanics ; Volume 48, Issue 7 , 2015 , Pages 1241-1247 ; 00219290 (ISSN) ; Manuchehrfar, F ; Rafii Tabar, H ; Sharif University of Technology
Elsevier Ltd 2015
Axon is an important part of the neuronal cells and axonal microtubules are bundles in axons. In axons, microtubules are coated with microtubule-associated protein tau, a natively unfolded filamentous protein in the central nervous system. These proteins are responsible for cross-linking axonal microtubule bundles. Through complimentary dimerization with other tau proteins, bridges are formed between nearby microtubules creating bundles. Formation of bundles of microtubules causes their transverse reinforcement and has been shown to enhance their ability to bear compressive loads. Though microtubules are conventionally regarded as bearing compressive loads, in certain circumstances during...