BCHM-3050 Study Guide - Midterm Guide: Buffer Zone, Protein Folding, Ramachandran Plot

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Study Guide Exam 1 Bio Chemistry 3050
Water
1. Understand the properties of water and how hydrogen bonding influences them
Water is polar covalent
Between 2 different water molecules, you have hydrogen bonds (weakest bonds)
Understand that if you add solutes to water (NaCl for example) you will increase
the boiling point and decrease the freezing point. This because the bonding in
NaCl is stronger and needs more energy to be broken apart.
2. What is osmotic pressure?
The pressure required to stop the net flow of water across the membrane. This
pressure is exerted to counteract the forces that are caused by osmosis
Osmosis- water movement from LOW concentration HIGH concentration
3. Explain isotonic, hypotonic and hypertonic solutions
Isotonic balance of solute concentration inside and outside the red blood cell
Hypotonic concentration of solute inside the RBC is less than the concentration
outside.
If too much water leaves, the RBC can shrink
Hypotonic concentration of solutes inside the RBC is high than the
concentration outside.
If too much water enters, the RBC can burst
4. Be able to calculate pH or H+ ion concentration of a strong acid
Equations to memorize:
pH = -log [H+]
pOH = -log [OH-]
pH + pOH = 14
5. Understand the significance of buffers and know the Henderson-Hasselbalch equation
Buffers regulate pH. This is essential for all living things.
Buffers help maintain a constant hydrogen ion concentration
Buffer zone where the pH is not changing because the weak acid and conjugate
base are maintaining equilibrium at a certain concentration. This is when buffers
are most effective
Henderson-Hasselbalch equation:
[A-] conjugate base
[HA] weak acid
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Amino Acids
1. Defie o desie the Cetal Doga i elatio to the stoage & etieal of geeti
information, the creation of proteins and the expression of traits.
Central Dogma explains the storage, retrieval and expression of DNA
Proteins start folding as they form during translation
2. Illustrate and/or describe the general structural, physical and/or chemical characteristics
of amino acids.
Every amino acid has:
1. An amino group
2. A carboxyl group
3. An R group
The R group is what is makes each of the 20 amino acids unique. The properties
of the R goup deteies a aio aid’s lassifiatio. Depedig o the R
group, you can classify amino acids into 4 groups
1. Neutral nonpolar hydrophobic
2. Neutral polar - hydrophillic
3. Acidic extra carboxyl group
4. Basic extra amino group
Have the structures, three letter and one letter abbreviation of the 20 amino
acids memorized. Also which are essential and which are not.
3. Desie ad/o illustate the titatio of a aio aid, iludig the pI’s o pK’s of
ionizable groups.
Isoelectric Point (PI) the pH when a particular molecule carries no net charge
For hydrophobic (non polar) amino acids, there are only 2 pK values. Average
them and divide by 2 to get the PI.
At pK1, the first buffer is used and 50% of protons are given up
At pK2, the last 50% of protons are given up
For acidic amino acids you can NOT just average pK1 and pK2. You have to
average the two that give you a 100% net charge of 0.
4. Determine the charge of an amino acid and a peptide at a certain pH (based on their pK
values).
check class notes, she worked out a few of these on the board during lecture
5. Determine at what pH an amino acid and peptides would have a particular charge
(Based on pK values)
check class notes, she worked out a few of these on the board during lecture
6. Identify and/or describe the structures & properties of the 20 standard amino acids.
have the 20 amino acids memorized
know which are polar/nonpolar/acidic/basic/ essential/non essential
7. Distinguish between essential vs. non-essential amino acids vs. non-standard amino
acids, including examples of the physiological roles
ill men phail to try valine
Non standard amino acids
1. Neurotransmitters
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