Lec05 - Structural Motif(Supersecondary structural elements...

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Structural Motif (Supersecondary structural elements) Found in many proteins Always have same 3D structure Usually has the same general function
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Calmodulin: one polypeptide, two domains, two motifs each
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Binding Ca causes conformational change: new lowest energy state
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Protein functions are determined by their combination of domains Many proteins have multiple domains, each with specific functions Dehydrogenases NAD+ binding domain Substrate binding domain and catalytic site This domain varies with different enzymes Regulatory proteins cAMP binding domain DNA binding domain
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CAP Protein large domain: transcription activation small domain: DNA binding
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DNA cAMP Dimer: coiled-coil holds two polypeptides together
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Quaternary Structure # number and size of polypeptides in a functional protein hemoglobin - 2 alpha chains, 2 beta chains
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Homo: both polypeptides identical Hetero: non-identical polypeptides
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Denaturation and refolding of RNase A Denature: break all non-covalent bonds with heat or detergent, reduce disulfide bonds with reducing agent
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Commonly used reducing agents
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Some proteins need chaperones to fold properly in the cell Some chaperones are heat shock proteins:
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Protein Function Binding Proteins Catalysts Motor proteins
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