Titration Worksheet BIOC 423 Fall 2014
HINT: Some questions may or may not require more than one answer.
Problem #1: Titration of Glycine
1a) Which point (or points) has good buffering capacity? _
A, C, E
1b) Which point (or points) has poor buffering
EXAM 1 REVIEW
Be able to describe the chemical basis for each of the following noncovalent
-Hydrogen bonds: electrostatic attraction between the partial charges on
oxygen (-) and hydrogen (+)
-Electrostatic interactions: repu
-Be able to compare and contrast the structure, overall function, and oxygen binding
properties of hemoglobin and myoglobin.
o Single polypeptide of 153 amino acids
o None of the amino acid side chains are able to adequately bind and
CITRIC ACID CYCLE, REGULATION OF CAC, GLYOXYLATE CYCLE
Understand the overall reaction of the pyruvate dehydrogenase complex. Where is it
located? What coenzymes are integral to this complex?
Makes carbon in pyruvate available for the CAC
o The bridge be
Regulation of Gene Expression I
-At what points in the synthesis of a gene product can the process be regulated? What are
the most common points of regulation?
Makes sense to do most of the control at the very beginning of the process to save time
The Genetic Code
A few important facts:
o -Translation will occur in the cytoplasm (of eukaryotes)
o -It takes place on the ribosomes
o -It requires the presence of the mRNA, tRNAs, ribosomes, all 20 of the
individual standard amino acids you so diligentl
Regulation of Gene Expression II
Why are some genes (almost) always expressed?
What types of interactions govern the binding of regulatory proteins to DNA?
o Two short alpha-helices connected by a beta turn
o ~20 animo acid residues lon
Be able to:
-Know (be able to draw and/or recognize their structures) the 20 amino acids found in
proteins that are coded for by the genetic code: know the 3-letter abbreviation for each.
-Classify the amino acids as nonpolar, polar and uncha
Integration of Metabolism:
Pull everything together!
The Long Run
Well take a look at all the metabolic processes that take place in your body during, and
after a Sunday long run.
These processes include:
o -glycolysis/ gluconeogenesis/ glycogen metabolis
Fatty Acid Synthesis
Understand the role of fatty acid synthesis in intermediary metabolism.
Fat is an excellent storage form of energy
o -Excess fatty acids from diet can be incorporated into triacylglycerols (TAGs) in
o -Excess carbohydrates
Be able to draw the various glycosidic bonds present in glycogen.
Glycogen contains both 14 and 16 glycosidic bonds that puts many branches in
the glycogen molecule and creates thousands of non-reducing ends of the molecule
o Starch o
-Review First and Second Laws of Thermodynamics.
First Law: Energy is conserved
Second Law: Entropy increases (more disorder/ways to organize)
-Be able to use G as an index as to whether such reactions proceed spontaneously.
Negative = ex
What are the requirements (necessary ingredients) for bacterial DNA replication? What
are the rules?
A. DNA synthesis is semiconservative.
Conservative: Two parent strands stay together, and two daughter strands stay together.
Why are the various levels of chromosome organization necessary?
There are large amounts of DNA.
o Very fragile, subject to shear damage if unprotected.
Not all of it is (or ought to be) available for expression at all times;
o some is pac
Amino Acid Catabolism I and II
Understand the general pathway for the breakdown of all amino acids; where does
each step occur in the human body?
First, carbon skeletons split from amino groups
o Both take different routes
1. Transfer of am
-What are the roles of nucleotides-why do we care about their synthesis and
Nucleotides play a variety of important roles in all cells.
o They are the monomers of DNA and RNA.
o They are essential carriers of chemical e
Gluconeogenesis and The Cori Cycle
Understand the role of gluconeogenesis in normal physiological processes
at 7 steps, the reverse of glycolysis
an anabolic pathway (biosynthetic)
synthesizes glucose from nonhexose precursors.
occurs primarily in liv
Describe the structure of the peptide bond, showing geometry, charge distribution and Hbonding groups.
Rigid and planar
Draw the peptide backbone of a 5-residue portion of a protein.
Compare and contrast primary, secondary, tertiary and
Pentose Phosphate Pathway
AKA: Hexose Monophosphate Shunt; (HMS) Hexose Monophosphate Pathway (HMP)
Understand the functions, active tissues, control of the pentose phosphate pathway
At this point in the course we have encountered two different forms of r
Be able to determine the change in reduction potential, and therefore the change in free
energy, of a reaction (SEE APPENDIX)
Understand the physical organization of components of the electron transport chain.
Be able to diagram
Be able to describe the general biochemical and functional properties of signal
o Signal molecule fits binding site on its complementary receptor and other
o When enzymes ac
Membrane Structure and Transport Proteins
Outline the structural features of membranes that are generally shared by all
Caused by hydrophobic and Van der Waals interactions between the
Be able to describe the chemical basis for each of the following non-covalent chemical
interactions, and know the relative strengths of each: (Covalent bond = 350-450 kJ/mol)
In the case of water, either the oxygen atom acts as a hy
Protein Synthesis: Translation
How are amino acids activated and linked to tRNAs? Why this is necessary, and
what are the energetic costs involved?
o Activation or charging = attachment of AA to tRNA = aminoacylation
o Amino ac
Understand the difference between the structures of aldoses and ketoses.
Aldose = aldehyde sugar
Ketose = ketone sugar
Be able to draw the structures of glucose and fructose.
Know the structures of the disaccharides sucrose and
RNA: Structure, Function, Metabolism
Describe the three major RNA species in terms of their structure and function
Transfer RNA (tRNA)
o is a small (65-110 nucleotides) molecule designed to carry activated amino
acids to the site of protein synthesis, the
Enzyme Kinetics and Inhibition
-Be able to define and explain each of the terms and all the assumptions of the MM
Rate of formation of ES = k1[E][S]
Rate of disintegration of ES = (k-1 +k2)[ES]
V0 = rate that product
Lipid bylayer formed by lipids and glycolipids due to their ampipathic nature.
Fluidity; different at varying temperature; determined by number of cis-bonds and moderated or
bolstered by cholesterol
Membrane protein; varie in function and distributi
What characteristics do biomolecules, in general, and proteins, specifically, have that can be used
Affinity (what does the protein like to bind to?)
Be able to describe the rationa
Intro to the Course and Water OBJECTIVES Be able to describe the chemical basis for each of the following non-covalent chemical interactions, and know the relative strengths of each: -Hydrogen bonds -Electrostatic interactions -van der Waals interact