NEUR 2200 Lecture Notes - Lecture 25: Chronobiology, Neurodegeneration, Frontal Lobe
28 Feb 2017
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Document Summary
Proteins: sequence of amino acid residues makes up a proteins (dna mrna) Dna is transcribed the mrna with the nucleus and then leaves the nucleus to be translated. Then the mrna is translated to and amino acid sequence. The sequence is modified by post transitional modifications (alters physical and chemical properties: folding causes secondary tertiary, quaternary structures (due to negative and positive charges) Native conformation: how the protein naturally folds. Proteins can go through several conformational changes (primary secondary) in order to perform functions (caused by a substrate binding to the active sit of enzymes) Glycosylation: effects on protein folding, stability and activity. It is the folded structure of a protein that makes it capable of performing its biological function. Misfolding shape changes in proteins contribute to neurodegenerative diseases. When folded proteins bounce back to being unfolded and chaperones do not fold them back the unfolded proteins are at a high energy state.
