[BIOCHEM 420] - Midterm Exam Guide - Everything you need to know! (99 pages long)

• School: UMASS-Amherst
• Department: Biochemistry & Molecular Bio.
• Course: BIOCHEM 420
• Professor: Becky Miller

Document Summary

Primary structure: order of amino acids no folding, resonance structures: movement of electrons moved between multiple atoms, peptide bonds (covalent): link amino acids together. Hemoglobin: two sets of identical polypeptides (4 chains) to final structure. Polypeptide and protein are two distinct things. Secondary structure: amino acids start to take on shapes alpha helices & beta sheets. Tertiary structure: alpha helices and beta sheets are folded and r groups interact defines final structure. Quaternary structure: exists for some proteins but not all if there is more than one polypeptide chain. What is the charge of aspartic acid at ph= 8. 0: need to decide if it is protonated or derogated. Approach: assess whether the n-terminus, c-terminus, and each group is protonated or deprotonated. Then, determine the charge for each functional group. Once you have done this, add all the charges together to determine the net charge: using the pka, table provided, estimate the net charge of the following peptide at ph=12.