LS3-8-10 - Lecture 8 Protein Function Protein Folding...

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Lecture 8 Protein Function Protein Folding Protein Degradation Antibody - structure, use in Molecular Biology Allison: p93-106 p251-257
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Fig 5.12 Protein activity is regulated at many levels Folding Rate of synthesis { Stability Decay
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Fig 5.12 Protein activity is regulated at many levels
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Fig 5.11 Enzymes lower activation energies Induced fit model
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Fig 5.12 Allosteric regulation Negative Positive
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Primary Secondary Tertiary Quarternary
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A protein folds to form a specific 3-D conformation according to its sequence. The center of a protein is usually hydrophobic and the exterior of a protein is usually hydrophilic. Spontaneous folding Some proteins can fold to their native conformation (with the lowest free energy) spontaneously after synthesis. Chaperone-assisted folding Some proteins may not appropriately fold by themselves, they need help of chaperones, many “heat shock” (hsp) proteins are chaperones Denature Loss of native folding due to breakage of weak (H, ionic etc) or strong (S- S) bonds, by heat, freezing/thaw, extreme pH or ionic conditions, detergents, reducing agents, etc. Denatured proteins are often insoluble. Renature Restoration of the native conformation (and solubility in aqueous solution) Protein folding
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Figure 3-5 Molecular Biology of the Cell (© Garland Science 2008)
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Figure 3-6a Molecular Biology of the Cell (© Garland Science 2008)
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This note was uploaded on 04/26/2010 for the course LS 252-009-20 taught by Professor Chen during the Spring '09 term at UCLA.

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LS3-8-10 - Lecture 8 Protein Function Protein Folding...

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