Browsing University of Waterloo by Subject "protein folding"
Now showing items 1-5 of 5
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Folding and Stability Studies on Amyotrophic Lateral Sclerosis-Associated apo Cu, Zn Superoxide dismutases
(University of Waterloo, 2009-10-05)Amyotrophic lateral sclerosis (ALS) is a debilitating, incurable, neurodegenerative disease characterized by degradation of motor neurons leading to paralysis and ultimately death in ~3-5 years. Approximately 10% of ALS ... -
A Minimal Model for the Hydrophobic and Hydrogen Bonding Effects on Secondary and Tertiary Structure Formation in Proteins
(University of Waterloo, 2009-04-30)A refinement of a minimal model for protein folding originally proposed by Imamura is presented. The representation of the alpha-helix has been improved by adding in explicit modelling of the entire peptide unit. A four-helix ... -
Stability and Strain in Hisactophilin and Mechanism of the Myristoyl Switch
(University of Waterloo, 2019-05-23)Hisactophilin is a myristoylated, histidine-rich, pH-dependent actin- and membrane-binding protein. In response to cellular changes in pH, this β-trefoil protein reversibly switches between cytosolic and membrane- bound ... -
Structure of Human Cu, Zn Superoxide Dismutase-1 Inclusion Body Aggregates using Quenched Hydrogen-Deuterium Amide Exchange
(University of Waterloo, 2021-12-22)Inclusion bodies (IBs) are insoluble protein aggregates that can be formed within recombinant bacteria. These aggregates, once thought to be an obstacle in recombinant protein expression and purification, have recently ... -
Thermodynamics, kinetics and inclusion body formation of a de novo designed protein Threefoil
(University of Waterloo, 2014-01-28)Threefoil is a small engineered protein of 141 amino acids which is a member of the beta-trefoil superfamily, with three-fold symmetry and high thermal and kinetic stability. Its primary sequence was designed based on a ...