Biological Chemistry Study Guide Exam 1
Biological Chemistry Study Guide Exam 1 CHEM 2770
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This 6 page Study Guide was uploaded by Corey Burr on Thursday February 4, 2016. The Study Guide belongs to CHEM 2770 at East Carolina University taught by Dr. Colin Burns in Spring 2016. Since its upload, it has received 122 views. For similar materials see Biological Chemistry in Chemistry at East Carolina University.
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The content was detailed, clear, and very well organized. Will definitely be coming back to Corey for help in class!
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Date Created: 02/04/16
Study Guide for Biochemisty Exam 1 Classification Name and Structure Serine Cysteine Asparagine Threonine Polar Amino Acids Glutamine Tyrosine Study Guide for Biochemisty Exam 1 Methionine Valine Alanine Leucine Non- Polar Amino Acids Isoleucine Phenylalanine Tryptophan Proline Glycine Study Guide for Biochemisty Exam 1 Arginine Lysine Basic Histidine Amino Acids Glutamic Acid Aspartic Acid Acidic Amino Acids 1. How can you tell if an amino aci_____________ACIDIC? _____________________ 2. How many amino acids are classified as Polar? ____ Non-polar? _____ Acidic? ____ Basic? _____ 3. Amino Acids are the building blocks of what biomolecule? __________________ 4. What are the four classes of biomolecules? ______________________________________________ 5. If the pKa of a molecule is LARGER than the pH of the solution, which form of the molecule, acidic or basic, is predominant in solution? _______________ What about if the pKa is SMALLER than the pH? __________________ Study Guide for Biochemisty Exam 1 6. What is the difference between prokaryotic and eukaryotic cells? _____________________________ 7. What is the “central dogma” of biology? __________________________________________________ 8. Put the following in order by increasing bond strength: hydrogen bonds, van der Waals interactions, electrostatic (ionic) bonds. 9. Non-polar molecules interacting with one another in the presence of water is known as what? ______________________ 10. When nonpolar molecules are removed from water, what happens to the entropy of water? 11. KNOW the Henderson-Hasselbalch equation and what is used to calculate. 12. For BASIC amino acids, which form, protonated or deprotonated, predominates at a neutral pH (~ 7)? _________________ 13. For ACIDIC amino acids, which form, protonated or deprotonated, predominates at a neutral pH (~ 7)? _________________ When going from a deprotonated to protonated form of amino acid, the (-) charge on the O turns into OH and the NH turn2 into NH . Exam3le: 14. What two pieces make up a secondary structure of a protein? 15. What stabilizes an alpha helix? 16. In proteins, all alpha helices are which way: Left handed (counter clockwise) or right handed (clockwise) ? 17. What are beta sheets made up of? 18. What is the proteome? - Look at 3 letter abbreviations for amino acids - Know how to form a peptide bond from the given information Study Guide for Biochemisty Exam 1 - Know what is meant by primary, secondary, tertiary, and quaternary structures. - Know the steps in understanding the proteome (isolating, characterizing, and cataloging proteins) - Know ion-exchange chromatography, gel-filtration chromatography (size separation), dialysis, affinity chromatography, and gel-electrophoresis. Study Guide for Biochemisty Exam 1 Answer Key: 1. Basic Amino Acids have a positive net charge. Acidic amino acids have a negative net charge. (look at structure) 2. Polar: 6 Non-polar: 9 Acidic: 2 Basic: 3 3. Proteins 4. Proteins, carbohydrates, nucleic acids, and lipids 5. ACIDIC / BASIC 6. Eukaryotic cells have membrane bound organelles where prokaryotic cells do not. Prokaryotic cells are much simpler cells. 7. It basically explains the process of DNA replication through transcription into RNA then translated back into DNA in order for new molecules to be formed. 8. Weakest -> van der Waals < Hydrogen bonds < Ionic bonds -> Strongest 9. The hydrophobic effect 10.Entropy of water increases when they are removed 11.pH = pKa + log ([A ]/[HA]) ; used to find concentrations of acid and base in solution 12.Protonated 13.Deprotonated 14.Alpha helix and Beta sheet 15.Hydrogen bonds between the amine (NH) groups and the carbonyl groups (CO). 16.Right handed; they are favored energetically. 17.Polypeptide chains come together to make beta strands which then bond to each other by hydrogen bonds to form beta sheets. Run in parallel or antiparallel directions or can be mixture. 18.It is the collection of proteins expressed by the genome.
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