BS 161 Lecture Notes - Lecture 3: Partial Charge, Hydrogen Bond, Ionic Bonding

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12 Feb 2019
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Partial charge due to difference in electronegativity between o" and h". Found in: carbohydrates, proteins, nucleic acids, lipids. Ex. found in ethanol, makes it soluble in water. Partial charge due to difference in electronegativity between o" and c". Ex. found in peptide bonds and helps proteins fold and stay soluble in water. Frequently lose a proton to become negatively charged. The end of a protein, which is called the c-terminus, always has a carboxyl group. Frequently gain a proton to become positive. The beginning of a protein, which is called the n- terminus, always has an amino group. Due to the s" and h" being similar in electronegativity, there is little hydrogen bonding, and are less soluble in water. S-h reacts with s-h to form s-s (disulfide bonds). The formation of s-s bonds normally stabilizes protein structure by covalently cross-linking different parts of the protein together. The crosslinking that occurs in fried eggs is in part through sulfhydryl group.

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