BIOL 112 Chapter 4: Proteins – Structure and self-assembly

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29 Nov 2016
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BIOL 112 Full Course Notes
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BIOL 112 Full Course Notes
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The e(cid:454)a(cid:272)t order of a(cid:373)i(cid:374)o a(cid:272)ids i(cid:374) a protei(cid:374) deter(cid:373)i(cid:374)es the protei(cid:374)"s shape a(cid:374)d fu(cid:374)(cid:272)tio(cid:374). R groups makes amino acids differ from one another in their chemical and physical properties. Structures of 20 amino acids commonly found in proteins (annotate on printout of structures) Properties that strongly influence how a polypeptide folds 3d shape of the protein. Whether they are hydrophobic or hydrophilic spe(cid:272)ial (cid:272)hara(cid:272)teristi(cid:272)s that (cid:373)ight affe(cid:272)t a protei(cid:374)"s stru(cid:272)ture. Do not readily interact with water or form hydrogen bonds. Have a permanent charge separation one end of the r group is slightly more negatively charged than the other tend to form hydrogen bonds with each other or with water molecules (hydrophilic) At the ph of a cell the r groups of the basic amino acids gain a proton and become positively charged the r groups of the acidic amino acids lose a proton and become negatively charged. Usually located on the outside surface of the folded molecule.

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