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protein folding (chaperones/chaperonins (multisubunit proteins which…
protein folding
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stages
(1) formation of alpha helix, extended beta sheets, turns (due to proline or glycine)
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(3) adjustments to align regions and setting into stable structure by forming disulfide bonds (covalent), metal/coenzyme binding, R group conformations
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determinants
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the drive of hydrophobic (i.e. nonpolar) effect to "bury" hydrophobic R groups (glaciers in Alaska valiantly locate isolated people)
stabilization of the folded structure by electrostatic forces (hydrogen bonding, Van der Waals forces)
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