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Lecture

BIOCH 200 (January 31, 2014) - Protein Structure and Function

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Department
Biochemistry
Course
BIOCH200
Professor
Walter Dixon
Semester
Winter

Description
BIOCH 200 Protein Structure and Function – The Amino Acids (con’t) + Peptide Bonds and Primary Structure (January 31, 2014) • Histidine (His) o The side chain will either contain an imidazolium ion (protonated) OR an imidazole (deprotonated) depending on the pH  This conversion is gradual though: • The more acidic the surrounding environment, the more imidazolium-ion-containing side chains you will have (more protons = higher chance of protonation) • The more basic the surrounding environment, the more imidazole-containing side chains you will have (less protons = higher chance of deprotonation) Charged Amino Acids (they are charged and therefore, also polar) • Aspartate (Asp) o Has a second carboxyl group on the side chain  Therefore, it has an overall negative charge (pH = 7) and acts like a acid -  COO is a H-bond acceptor (because there is no covalently bonded hydrogen to the electronegative atom)  @ pH = 1 (conversion initiates at pH = 4) • Aspartate  aspartic acid o Because carboxyl group get protonated and becomes a carboxylic acid • Glutamate (Glu) o Structure is almost exactly the same as that of aspartate BUT it has an extra carbon on the side chain o It has the same properties as Aspartate as well  @ pH = 1 • Glutamate  Glutamic Acid • Lysine (Lys) o Side chain = 4 carbons and an amino group
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