MBB222-lecture7

MBB222-lecture7 - Tertiary Structure: the overall...

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Tertiary Structure: – the overall conformation / 3-D arrangement of a polypeptide chain abilization as a result of hydrophobic interactions between – stabilization as a result of hydrophobic interactions between nonpolar side chains, hydrogen bonds between polar side chains, ionic interactions, Van der Waals forces, and also covalent bonds – hold elements of secondary structure compactly together ot rigidly fixed (most stabilizing interactions are weak) and – not rigidly fixed (most stabilizing interactions are weak) and thus undergoes continual minute fluctuations »important consequences in terms of both function and regulation
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Tertiary Structures of a GDP-Binding Protein
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• Domains : – modules of tertiary structure – structural domains: » e.g., a proline-rich domain, an acidic domain nctional domains: functional domains: » e.g., a DNA-binding domain, a kinase domain – illustrates the principle of complex molecules being built from simpler components • Motifs : – particular combinations of secondary structures that build up the tertiary structure of a protein undreds have been discovered – hundreds have been discovered – often signatures for a specific function
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– e.g., zinc finger nsists of an - » consists of an α helix and 2 β strands with antiparallel it t i f i orientation, forming a finger-like bundle, held together by a zinc ion » formed by ~30 ino acid residues amino acid residues » commonly found in proteins that bind nucleic acids
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– e.g., leucine zipper
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This note was uploaded on 12/13/2011 for the course MBB 201 taught by Professor -- during the Spring '11 term at Simon Fraser.

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MBB222-lecture7 - Tertiary Structure: the overall...

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