BIOCHEM 3G03 Chapter Notes - Chapter 4: Protein Structure, Van Der Waals Strain, Protein Folding

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Essence of proteins biological function is their interaction with other molecules. Protein: consists of one or more polypeptides (chains of polymerized amino acids) The 20 amino acids have different chemical properties. R groups can be hydrophobic, polar or charged. -amino acids: a(cid:373)i(cid:374)o + (cid:272)a(cid:396)(cid:271)o(cid:454)(cid:455)late g(cid:396)oups a(cid:396)e atta(cid:272)hed to a (cid:272)e(cid:374)t(cid:396)al (cid:272)a(cid:396)(cid:271)o(cid:374) ato(cid:373): (cid:272)a(cid:396)(cid:271)o(cid:374) c . 19/20 standard aa = asymmetric/chiral: chirality results from as(cid:455)(cid:373)(cid:373)et(cid:396)(cid:455) of the c , four different substituents can be arranged in two ways. Aa in protein = left (l amino acids) Two forms are physically indistinguishable and usually present in equal amounts in synthetic preparations but they behave differently in biological systems. Hydrophobic amino acids are located in the interior of the protein molecule do not directly participate in mediating chemical reactions. Found on the solvent-exposed surface but can also occur in the interior (as long as h bond requirements are satisfied)

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