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Integral proteins can be linked to lipids, eg fatty acids and prenyl groups, on the
cytosolic side of the bilayer.
Lipid linked non cytosolic side proteins are made with transmembrane segment
which is cleaved off and glycosylphosphatidyl (GPI) anchor is added these
proteins can be readily distinguished by Phosphatidylinositol-specific
Phosphokinase C, an enzyme.
Beta barrels are largely restricted to bacterial, mitochondrial and chloroplast
outer membranes. Each beta strand is bound tightly to its neighbours by
hydrogen bonds making it difficult to manipulate for conformational changes
making it hard to be an open/shut ion channel.
Reducing environment of cytosol means that disulphide bonds between cysteine
does not happen only happens on non-cytosolic side and essential for
stabilizing structure or association with other polypeptides.
Transmembrane proteins can be solubilised and purified in detergents, can then
be analysed using SDS polyacrylamide-gel electrophoresis.
Diffusion of membrane proteins proved using heterocaryons with labelled
proteins. FRAP and FLIP techniques used.
Lipid confinement limited to outer layer of membrane.
Cell coat, glycocalyx, is the carbohydrate rich zone on cell surface. protect
membrane + used in cell to cell recognition.
Restruction of movement of proteins in membrane = scaffolding proteins, lipid
rafts, attachment to macromolecules, assemble into large aggreagates,
interactions with proteins on another cell membrane.
Spectrin a protein attached to cytoskeleton and is noncovalently attached to the
membrane by association with Ankyrin, a protein attached to the cytosolic
doman of protein band 3. Band 4.1 protein binds to spectrin, actin as well as
cytosolic domain of band 3 and glycophorin.
Distrubed protein localisation can lead to disorders. In healthy cardiac myocytes,
calcium ion channels are arranged in a regular array though this can break down
in heart failure. Arrangement as well as presence of ion channels is important for
normal cell function.