Phospholipid structure

Amphipathic molecule (phosphatidyl choline) hydrophobic part: fatty acids hydrophilic part: phosphate & choline

Membrane structure

Membrane components

Transmembrane proteins

Intercellular structures
Desmosomes spot welds, dense proteins (cytoplasm & intercellular) fibers (intermediate filaments) extend across cells epithelial cells (especially skin), cardiac intercalated disks Tight junctions cell collar, block large molecules, no lateral protein movement epithelial cells Gap junctions cell-cell communication, small molecules (<1000 MWt) cardiac intercalated disks, smooth muscle
5

Desmosomes
spot welds, dense proteins (cytoplasm & intercellular)

fibers (intermediate filaments) extend across cells

epithelial cells (especially skin), cardiac intercalated disks

fig 3-10a
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Tight junctions
cell collar, block large molecules, no lateral protein movement

epithelial tissue (esp. kidney, gut)

paracellular pathway between cells

fig 3-10b

Gap junctions
cell-cell communication, small molecules (<1000 MWt) cardiac intercalated disks, smooth muscle

fig 3-10d
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Epithelial cell
fig 3-10c

Protein ligand interaction

Proteins could be: enzymes receptors transporters Ligands would be: substrates, allosteric regulators chemical messengers transported substances

transcription factors
any of above

transcription regulators
drugs

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Protein-ligand binding properties

Specificity: binding depends on ligand size, shape, charge Affinity: strength of binding: i.e. [ligand] at 50% binding Saturation: there is a finite number of binding sites Competition: structurally similar molecules can compete for binding

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Specificity
binding depends on ligand size, shape, charge

fig 3-26

fig 3-27

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Specificity
protein Y specificity greater than protein X specificity

fig 3-28
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Affinity
strength of binding: i.e. [ligand] at 50% binding

fig 3-29
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Affinity & saturation

strength of binding: i.e. [ligand] at 50% binding

fig 3-30
15

Affinity (different proteins)

strength of binding: i.e. [ligand] at 50% binding

fig 3-31
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Affinity (different ligands)

strength of binding: i.e. [ligand] at 50% binding

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Protein-ligand binding properties

Specificity: binding depends on ligand size, shape, charge Affinity: strength of binding: i.e. [ligand] at 50% binding Saturation: there is a finite number of binding sites Competition: structurally similar molecules can compete for binding

and remember: the protein can be an enzyme, receptor, transporter, etc.

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Regulating binding site properties

a. Allosteric modulation reversible binding at another (allo-) site can be activation or inhibition

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Regulating binding site properties

a. Covalent modulation chemical alteration of the protein can be activation or inhibition

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Metabolism (pathways)

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Metabolism (key)
Key: A: glycogenesis, B: glycogenolysis, C: glycolysis, C+D: anaerobic glycolysis (lactic acid fermentation), E: gluconeogenesis, F: irreversible step (pyruvate dehydrogenase), G: protein synthesis, H: proteolysis, I: lipogenesis, J: lipolysis, K: Krebs cycle, L: urea synthesis, M: ketogenesis Anabolic pathways: A, G, I Catabolic pathways: B, C, E, F, H, J, K Liver only: E, L, M Mitochondrial: K Ribosomal: G Smooth endoplasmic reticulum: I

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Energy content

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