Membrane Proteins & Structures, Cellular Imaging

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Department
Biochemistry & Molecular Bio.
Course
BIOCHEM 524
Professor
David Gross
Semester
Spring

Description
March 3 Notes • typical single-pass integral membrane protein o single alpha-helical region transverses the lipid bilayer o protein has interchain disulfide bonds in extracellular matrix, exposed sulfhydryl groups in cytosol (reducing environment), also can have oligosaccharides attached extracellularly • bacteriorhodopsin structure o 5 alpha-helical transmembrane segments o rhodopsin is a protein in the eye o in its core retinal is linked to lysine o its exposed NH2 end is in the extracellular space, carboxyl end in the cytosol • beta-barrel membrane proteins o commonly found in bacteria, mitochondria & chloroplast membranes o barrel can consist of different number of beta-strands o very difficult to predict beta-barrel structure b/c of the way beta-strands interact • beta-sheet structure o can be parallel (same ends facing same way) or antiparallel (ends facing opposite ways) o form wavy pattern • membrane protein anchoring o covalent linkages form to lipid molecules  amide linkage between terminal amino group & myristic acid  thioester linkage between cysteine & palmitic group  thioester linkage between cysteine & prenyl group • integral membrane proteins o when exposed to surface, commonly glycosylated (sugar residues) o different types:  transmembrane proteogylcans  transmembrane glycoprotein  adsorbed glycoprotein – not integral, connects w/ integral proteins o connect w/ glycolipids in lipid bilayer • visualizing cell organization & dynamics o localization to specific cellular compartments or regions o visualization of cellular structures o dynamics of molecular movements o molecular interaction & co-localization • light microscopy
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