BioMG 3350 Amino Acid Classifications - Quiz 1
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
|
|
||||
|---|---|---|---|---|---|
| Glycine (Gly) | Nonpolar alipathic
Provides least amount of steric hindrance in proteins
Not particularly hydrophobic
🗑
|
||||
| Alanine (Ala) | Nonpolar alipathic
Saturated hydrocarbon R group
Important in hydrophobic interactions
🗑
|
||||
| Proline (Pro) | Nonpolar alipathic
The only amino acid with a substituted alpha-amino group
Influences protein folding by forcing a bend in the chain
🗑
|
||||
| Valine (Val) | Nonpolar alipathic
Saturated hydrocarbon R group
Important in hydrophobic interactions
🗑
|
||||
| Leucine (Leu) | Nonpolar alipathic
Saturated hydrocarbon R group
Important in hydrophobic interactions
🗑
|
||||
| Isoleucine (Ile) | Nonpolar alipathic
Saturated hydrocarbon R group
Important in hydrophobic interactions
🗑
|
||||
| Methionine (Met) | Nonpolar alipathic
🗑
|
||||
| Phenylalanine (Phe) | Aromatic
Hydrophobic and neutral at any pH
🗑
|
||||
| Tyrosine (Tyr) | Aromatic
Has -OH group that contributes polarity and H-bond capability
Polar group makes it both hydrophobic and hydrophilic
Can be phosphorylated
🗑
|
||||
| Tryptophan (Trp) | Aromatic
Hydrophobic and neutral at any pH
🗑
|
||||
| Serine (Ser) | Polar uncharged
🗑
|
||||
| Threonine (Thr) | Polar uncharged
Has -OH group that contributes polarity and H-bond capability
🗑
|
||||
| Cysteine (Cys) | Polar uncharged
Can form disulfides in the right oxidizing conditions
🗑
|
||||
| Asparagine (Asn) | Polar uncharged
🗑
|
||||
| Glutamine (Gln) | Polar uncharged
🗑
|
||||
| Lysine (Lys) | Positively charged
🗑
|
||||
| Histidine (His) | Positively charged
The only amino acid having an R group with a pKa near 7
Important in the active site of some proteins
🗑
|
||||
| Arginine (Arg) | Positively charged
🗑
|
||||
| Aspartate (Asp) | Negatively charged
🗑
|
||||
| Glutamate (Glu) | Negatively charged
🗑
|
||||
| Peptide bond | It is substituted amide linkage
It is formed in a condensation reaction
🗑
|
||||
| Affinity chromatography | Taking advantage of unique structural or functional properties of a protein, this technique specifically removes the protein of interest from solution.
🗑
|
||||
| Electrophoresis | Proteins are separated on the basis of their ability to migrate in an electric field, an indicator of relative size.
🗑
|
||||
| Phosphorylation | The most common form of post-translational modification
🗑
|
||||
| Isometric point | Where the net charge on the amino acid is zero
🗑
|
||||
| pKa | the pH at which there is a 50:50 ratio of protonated/deprotonated species for a specific ionizable group
🗑
|
||||
| Chromatography | separate based on properties of protein charge, size, hydrophobicity
🗑
|
||||
| SDS Gel | Hydrophobic parts of the protein bind to the hydrophilic, negative parts of SDS, causing the protein to unfold. Then, a reducing agent is added to break the covalent disulfide bonds. Voltage is applied and they are ran through a gel.
🗑
|
||||
| Consensus sequences | Short stretches of highly conserved sequences
🗑
|
||||
| X-ray crystallography | Measure how the crystal diffracts x-rays
main limitation: crystals can be very hard to grow
🗑
|
||||
| Nuclear magnetic resonance (NMR) | Produce the protein using heavy-isotope labeled amino acids and then measure chemical shifts of protein in solution in an NMR machine.
main limitation: Currently limited to small-medium proteins <300 amino acids
🗑
|
||||
| Cryo-EM (electron microscopy) | Protein sits in different orientations in ice and is show with electron beam from above. A detector collects the shadows(electron density). Need large proteins >200kDa
🗑
|
||||
| Surface tertiary structure | Shows the solvent-accessible surface of the protein
🗑
|
||||
| Space-filling | Shows every (non-hydrogen) atom as a sphere with appropriate radius
🗑
|
||||
| Ribbon/cartoon | Traces the polypeptide backbone, highlights secondary structure
🗑
|
||||
| Hydrophobic effect | most important weak force for determining protein structure
🗑
|
||||
| two main movement constraints in peptides | planar peptide bond and steric hindrance
🗑
|
||||
| trans | 180 degrees
🗑
|
||||
| cis | 0 degrees
🗑
|
||||
| Ramachandran Plot | Shows permissible psi, phi angles
🗑
|
||||
| coil | structured but no pattern
🗑
|
||||
| loops | unstructured because of multiple configurations
becomes structured when bound to other proteins
🗑
|
Review the information in the table. When you are ready to quiz yourself you can hide individual columns or the entire table. Then you can click on the empty cells to reveal the answer. Try to recall what will be displayed before clicking the empty cell.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Created by:
10208321647500519
Popular Biology sets