NC STATE CHEM 430 - BIOCHEM Tutoring

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tutor told to me to watch out for the following supposedly he also likes to do select all that apply well basic acidic polar nonpolar aromatic If given sequence be able to 2 1 Memorize Amino Acids and be able to draw them 3 letter code and 1 letter code as a determine net charge at a given pH b calculate pI c Pointing out alpha helix residue n n 4 between N H and C O d Figure out the net charge at pH and pick the one with the most negative charge or pick a group that has sulfur knowing amino acid structure e Know which amino acid has an aromatic group absorbance 280 nm f Know which amino acid can hydrogen bond slide in lecture 2 or 3 that mentions hydrogen bond donors acceptors g S T M have OH but cannot proton exchange 3 Given the structure write 3 letter code sequence N C terminal 4 Alpha carbon aka chiral carbon Glycine is only one that is not chiral a Groups are carboxylic acid amino group R group and hydrogen 5 pI is when net charge 0 isoelectric point pH pI positive net charge pH pI 6 Understand conjugate base acid compared to another structure conj Base loses 1 negative net charge proton and conj Acid gains 1 proton 7 Given titration curve a How many pKa the plateau match an amino acid to it slide in lecture first and last plateau are amino group and C group 8 Given pH find H 10 pH 9 When given a structure indicate psi and phi and indicate peptide bonds 10 There is one question that is EXACTLY the same as the practice exam 11 Characteristics of the Rachmadan Plot a Select all that apply know how to read the plot b Which axis is what and what structures correspond to the clusters alpha on bottom beta on top other cluster on side is c What does it mean to have an empty part d Relate to thermodynamics somehow Stable is low energy 12 How to distinguish parallel and antiparallel a How to recognize them b Which one is more stable c Patterns of hydrogen bonding One has diagonal H bonds and the other has 13 Identify protein folding folding funnel and 3 models on Lesson 4 mutant globule which parallel straight is partially folded a Selecting whats involved 14 Need to know what kind of forces are responsible for what structures a Primary peptide bonding Secondary hydrogen bonding Etc 15 One question about ion exchange given amino acid know if cation or anion exchange and charge of resin just understand how to do column chromatography a Buffer is put through second and has to be opposite of amino acid to get it out b Buffer and amino acid need same charge for excahnge and resin has to be opposite of both c Similar to last slide one lesson 5 in class slides titled more IEX 16 Size Exclusion a Big elutes first small last 17 If I have 3 residue calculate the probability that primary sequence can form 20 n a Specifically said not to focus on the probability of CORRECT sequence but maybe just know 18 Know functions of Urea BME and SDS a A question that is similar to practice exam about lanes b Urea disrupts H bonds c BME disrupts disulfide bonds d Heat is only IRREVERSIBLE Urea BME and SDS are all reversible e SDS net neg charge mass to charge ratio breaks noncovalent bonds including 19 Question that is similar to the slide 2 slides back from the last one on Lesson 5 except opposite so given the drawing and finding the lanes 20 One question that asks to explain in one sentence exact same thing Vivien like the disulfide practice exam 21 Predominating species 22 Know the K folding K greater than equal to less than 1 1 u a Spontaneity exergonic K folding greater than 1 multiple choice 23 Delta G concepts and Delta H concepts no math


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NC STATE CHEM 430 - BIOCHEM Tutoring

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