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34 Cards in this Set
- Front
- Back
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Glycine
Gly G |
H
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Alanine
Ala A |
CH3
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Proline
Pro P |
C
NH2-CH2 CH2-Ch2 |
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Valine
Val V |
CH
CH3-CH3 |
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Leucine
Leu L |
CH2
CH2 CH3-CH3 |
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Isoleucine
Ile I |
CH2
CH3 |
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Methionine
Met M |
CH2
CH2 S CH3 |
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Phenylalanine
Phe F |
CH2
Benzene |
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Tyrosine
Tyr Y |
CH2
Benzene OH |
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Tryptophan
Try W |
http://www.google.com/imgres?um=1&hl=en&sa=N&biw=998&bih=500&tbm=isch&tbnid=-q1_M8IL8-21eM:&imgrefurl=http://quizlet.com/2855398/amino-acids-structure-to-full-name-flash-cards/&docid=mm--zNn3YU2dGM&imgurl=http://o.quizlet.com/i/lH61_bNO2rcnBjOay5HMoA_m.jpg&w=145&h=240&ei=-sZYUNfWFob_ygHl5oDgAQ&zoom=1&iact=hc&vpx=444&vpy=163&dur=334&hovh=171&hovw=104&tx=104&ty=128&sig=110032649384371304087&page=1&tbnh=144&tbnw=88&start=0&ndsp=11&ved=1t:429,r:2,s:0,i:81
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Serine
Ser S |
CH2OH
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Threonine
Thr T |
H-C-OH
CH3 |
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Cysteine
Cys C |
CH2
SH |
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Asparagine
Asn N |
CH2
H2N-C=O |
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Glutamine
Gln Q |
CH2
CH2 H2N-C=O |
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Lysine
Lys K |
CH2
CH2 CH2 CH2 NH3+ |
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Arginine
Arg R |
CH2
CH2 CH2 NH C=NH2+ NH2 |
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Histidine
His H |
CH2
C-NH-CH=N-CH=Cº |
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Aspartate
Asp D |
CH2
COO- |
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Glutamate/Glutamic Acid
Glu E |
CH2
CH2 COO- |
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Which amino acids have aromatic R groups? Are they hydrophilic or hydrophobic?
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Phenylalanine
Tyrosine Tryptophan *Hydrophobic |
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Which amino acids have positively charged R groups?
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Lysine
Arginine Histidine |
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Which amino acids are polar with uncharged R groups? Are they hydrophobic or hydrohilic?
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Serine
Threonine Cysteine Asparagine Glutamine *More hydrophilic than nonpolar |
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Which amino acids have negatively charged R groups?
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Aspartate
Glutamate |
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Which amino acids are nonpolar with aliphatic R groups? Are they hydrophilic or hydrophobic?
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Glycine
Alanina Proline Valine Leucine Isoleucine Methionine *Hydrophobic |
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What are the 2 types of ion exchange chromatography? Describe each in terms of its stationary phase and mobile phase.
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1. Cation exchange: stationary phase is negative so that it can interact with cations
2. Anion exchange: stationary phase is positive so that it can interact with anions |
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How is separation done in an ion exchange chromatography?
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The pH is gradually changed to create a pH gradient and/or a salt gradient can be created.
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Explain what size exclusion chromatography/ gel filtration is.
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It separates based on size. The solid phase is made up polymer beads with pores of a particular size. Large proteins cant enter the cavities so they come out first. Smaller proteins enter the cavities and are slowed down by their labyrinthine paths.
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Explain what affinity chromatography is. How is the protein of interest eluted?
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This is based on binding affinity. The beads in the column have a ligand attached to them: which is a group/molecule that binds to proteins. If a protein is added that has an affinity for this ligand, it binds to it and its movement through the column is slowed down.
Elution: done with a solution with a high concentration of either salt or the ligand. |
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Explain what isoelectric focusing is.
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A procedure used to determine the isoelectric point of a protein. A pH gradient is established. When a protein mixture is applied, each protein migrates until it reaches its pI. In an electric field, proteins move across gel.
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What is 2 dimensional electrophoresis?
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It combines isoelectric focusing and SDS electrophoresis. it separates proteins with the same molecular weight but differ pI or proteins with similar pI but different molecular weights.
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Explain what electrophoresis is. Explain what happens with SDS.
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It uses a polyacrylamide gel that acts as a sieve and slows the migration of proteins proportionately according to size and shape.
With SDS, the detergent adds negative charge, so charge doesn't matter anymore. It also partially unfolds proteins so the shape doesn't matter either. It separates based on mass only. |
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What is the activity of an enzyme?
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Activity refers to the total units of enzyme in a solution
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What is the specific activity?
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The number of enzyme units per milligram of total protein. It is a measure of enzyme purity and increases as the enzyme becomes more pure.
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