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

Hydrogen bonds interacnon of n h and co of the pepnde

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Unformatted text preview: interacNons within the protein •  There is a cost in conforma:onal entropy of folding the protein into one specific naNve fold Favorable InteracNons in Proteins •  Hydrophobic effect ∆G = ∆H – T∆S –  Release of water molecules from structured solvaNon layer around the molecule as protein folds increases the net entropy •  Hydrogen bonds –  InteracNon of N- H and C=O of the pepNde bond leads to local regular structures such as α- helices and β- sheets •  London dispersion –  Medium- range weak aXracNon between all atoms contributes significantly to the stability in the interior of the protein •  Electrosta:c interac:ons –  Long- range strong interacNons between permanently charged groups –  Salt- bridges, esp. buried in the hydrophobic environment strongly stabilize the protein Protein TerNary Structure •  Stabilized by numerous weak interac:ons between amino acid side chains –  Largely hydrophobic and polar interac:ons –  Can be stabilized by disulfide bonds •  InteracNng amino acids are not necessarily next to each other in the primary sequence. •  Two major classes –  Fibrous and gl...
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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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