BCHE 395-7 2014 Protein III-VI Structure & Folding

Structural hierarchy of proteins primary structure i

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Unformatted text preview: ased disorder, decreased order (– ∆S), decreased disorder, increased order Protein Folding •  Protein folding process is spontaneous (– ∆G) Decreased randomness Myoglobin 153 free amino acids •  1. There is an unfavorable conforma:onal entropy change (–∆S) inherent in protein folding because folding increases order ∆G = ∆H – T∆S Protein Folding •  Protein folding process is spontaneous (– ∆G) •  2. There is a favorable enthalpy change (–∆H) from intramolecular R- group interac:ons that form non- covalent bonds ∆G = ∆H – T∆S Protein Folding •  Protein folding process is spontaneous (– ∆G) This is known as the hydrophobic effect Fig. 2- 7a •  3. There is a favorable entropy change (+∆S) from burial of hydrophobic R- groups within the interior of the folded protein because there is a decrease in the order of water ∆G = ∆H – T∆S Protein...
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This note was uploaded on 03/02/2014 for the course BIOCHEMIST 395 taught by Professor Potenza during the Spring '14 term at NMSU.

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