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Full-Text Articles in Life Sciences
Investigating The Disorder And Compaction Of Designed Minielastin Using Nuclear Magnetic Resonance., Ma Faye Charmagne Aquino Carvajal
Investigating The Disorder And Compaction Of Designed Minielastin Using Nuclear Magnetic Resonance., Ma Faye Charmagne Aquino Carvajal
Electronic Theses and Dissertations
Minielastins are elastin-based proteins with alternating hydrophobic and cross-link modules similar to tropoelastin. Tropoelastin is the ~70 kDa soluble monomeric precursor of elastin. The extracellular matrix protein, elastin provides elasticity to tissues and organs such as lungs, arteries and ligaments. The elastic properties of natural elastin are believed to be entropic in origin. In vivo, the elastin matrix is approximately 50% water by weight. Without water, elastin is brittle and hard. Minielastins, like tropoelastin, undergo a liquid-liquid phase transition upon an increase in temperature. Factors such as hydrophobicity, chain length and concentration affect the coacervation temperature, Tc. The …
Calcineurin: From Activation To Inhibition, Erik C. Cook
Calcineurin: From Activation To Inhibition, Erik C. Cook
Theses and Dissertations--Molecular and Cellular Biochemistry
Calcineurin is a Ser/Thr phosphatase whose function is implicated in critical physiological processes such as immune system activation, fetal heart development, and long-term depression in neurons. Calcineurin has been implicated in the progression of Alzheimer’s disease and cardiac hypertrophy. It is not well understood how calcineurin is activated on a molecular level by Ca2+ and its activating protein calmodulin. Previous data from our lab show that calmodulin interaction induces the folding of the intrinsically disordered regulatory domain of calcineurin in two discrete and distant regions into α-helical conformations and that this folding is critical for complete activation of calcineurin. …
Structural Basis For Ternary Complex Formation Between Tau, Hsp90, And Fkbp51, Alexander Steven Barrett
Structural Basis For Ternary Complex Formation Between Tau, Hsp90, And Fkbp51, Alexander Steven Barrett
USF Tampa Graduate Theses and Dissertations
The accumulation of the microtubule associated protein tau has been implicated in several neurological disorders; however, its interaction with chaperones along its normal degradation pathway remains largely uncharacterized at single residue resolution. In this study, nuclear magnetic resonance (NMR) spectroscopy was used to probe the interaction between tau, the molecular chaperone Hsp90, and the immunophilin FKBP51. Resonance intensity changes were observed for specific residues in the heteronuclear single quantum coherence (HSQC) spectra of 15N-labeled tau in the presence of Hsp90 and/or FKBP51. Analysis of the HSQC spectra identified the two hydrophobic hexapeptide motifs located at residues V275 - K280 and …