BIOL-103 Lecture Notes - Lecture 4: Loess, Steric Effects, Carboxylic Acid
2 Jan 2017
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Proteins are the workers of life -> they do lots of things like enzymes, hormones, receptors, structure, motor, antibodies, transport, etc. The monomer (simple unit) of proteins are amino acids. Here is their general structure (ionized and non-ionized): There are 20 amino acids, defined by their side chains (r groups). The order of the amino acids (as well as the environment) defines the shape of the protein. The amino acids can be ionized or not the(cid:455) are(cid:374)"t stro(cid:374)g a(cid:272)ids or (cid:271)ases. Nonpolar amino acids: alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, tyrosine, glycine. These amino acids have nonpolar r groups because they have nonpolar c-h bonds. It"s true that so(cid:373)e of the(cid:373) ha(cid:448)e polar (cid:271)o(cid:374)ds, (cid:271)ut (cid:271)e(cid:272)ause most of the bonds are (cid:374)o(cid:374)polar, the(cid:455)"re still (cid:272)o(cid:374)sidered (cid:374)o(cid:374)polar. Asparagine and glutamine have amines and carboxyls but are not charged. Protein structure comes in four layers: primary structure- sequence of amino acids covalently bonded together:
