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Lecture 5

Lecture 5 proteins

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University of Toronto St. George
Stavroula Andreopoulos

Lecture 5 Text Notes Globular Proteins - globular proteins – named for their spherical shape - diverse protein structures to reflect a variety of functions – binding, catalysis, regulation, transport, immunity, cellular signalling - functional diversity is due to the large number of folded structures possible to adopt and the varied chemistry of the 20 common amino acids - globular proteins exist in many structures – nearly all contain α-helices and β-sheets folded into compact structures stabilized by polar and nonpolar groups - helices and sheets that make up the core of most globular proteins represents the starting point for protein folding - hydrophobic interaction and other noncovalent forces stabilize relatively unstable helices, sheets and turns in the folded protein - cores of most globular and membrane proteins consist of α-helices and β-sheets for the reason that the highly polar N-H and C=O moieties of the peptide backbone must be neutralized on the hydrophobic core of the protein – stabilize the polar groups - interior of the globular protein is constant and conserved in sequence and structure - surface of the globular protein is composed of the loops and tight turns that connect the helices and sheets of the protein core – helices and sheets may also be found on the surface - segments of protein that are neither helix, sheet, nor turn are considered coils or random coils – however they are just as organized as the defined structures but do not conform to any frequently recurring pattern – strongly influenced by side-chain interactions with the rest of the protein - hydrophobic core – region in which hydrophobic side chains cluster together away from the solvent - backbone – polypeptide backbone itself, excluding side chains Subunit Interaction at the Quaternary Level - many proteins exist in nature as oligomers - oligomer – complex composed of often symmetric noncovalent assemblies of two or more monomer subunits - most intracellular enzymes are oligomeric – composed of either a single type
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