BIOL 303 1nd Edition Lecture 4Outline of Last Lecture I. Macromoleculesa. H20b. ProteinsOutline of Current Lecture I. Proteins (cont)a. Amino Acidb. Protein StructuresCurrent LectureI. Proteinsa. Amino acid:i. Has a dramatic impact on pHii. Moving parts, they are machines at molecular levels (proteins)iii. Not like DNA which are double helix and are very simpleiv. Dehydration reactions are how amino acids are held togetherv. Example of 3 = tri-peptide (hold amino acids) happens on the ribosome. Every time a new amino acid is added, it will hold on to the –OH groupvi. Amino terminate (HN ------------COOH) Carboxyl terminateb. Protein Structuresi. Each protein has a different amino sequence. Primary dictates what shape it’s going to be and FUNCTION *1. Every single disease (inherited) is due to a single amino acid change **2. If you change an amino acid in the sequence then it can change into a whole different functionii. High amount of diversity and potential. (20^n – the amount of possible amino acid sequences)iii. Bond flexibility allows many/countless possible conformationsiv. Water is an important factor with proper folding, mostly because it reacts with every R groupv. Secondary and tertiary = 3D folding1. Hydrophilic/hydrophobic interactions of R-groups2. Bonds and interactions b/w R groupsThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.3. Interactions b/w nearby peptide bonds4. Praline5. Cofactors (Mg2+)vi. Chaperon proteins: helps the protein fold in the right direction. Helpful in really large sequences. Detects proteins that are folded incorrectly. Non-polar amino acids are more folded into the surface, that’s how chaperon proteins bind to.vii. Cystein: can from covalent bonds, only R group that can. Connects w/ a disulfide bond
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