Levels of Structure
Amino Acids
Dihedral Angles
Effects of pH
Misc.
100

The levels of structure found in proteins in order. 

What is primary structure, secondary structure, tertiary structure, and quaternary structure?

100

The 4 main groups of amino acids.

What are non-polar (hydrophobic), polar, positively charged (basic), and negatively charged (acidic) amino acids?

100

These bonds are planar.

What are peptide bonds?

100

As pH increases, this happens to amino acids.

What is deprotonation?

100

These things can cause denaturation (5 parts will accept 3/5).

What are extreme pH changes, temperature, miscible organic solvents, detergents, and certain solvents?

200

Common secondary structures found in proteins (4 structures).

What are a-helices, B-sheets, B-turns, and random coils?

200

The bond that joins amino acids in a polypeptide.

What is a peptide bond?

200

Rotation is allowed around these bonds in a polypeptide.

What is the alpha-carbon/amino bond and the alpha-carbon/ carboxyl carbon bond? 

200

At very low pHs (no OH added), amino acids will exist in this form.

What is fully protonated?

200

Tryptophan has these abbreviations (1 letter and 3 letters) and is this type of amino acid. 

What is are W, Trp, and a non-polar/ hydrophobic amino acid?

300

Tertiary structure describes this property of proteins.

What is the well-defined, three-dimensional fold adopted by proteins?

300

The stereoisomer amino acids predominately exist in.

What is an L absolute configuration? 

300

These are the names of the dihedral angles found in a polypeptide.

What are phi and psi?

300

The point at which amino acids have a net neutral charge on a titration curve.

What is the isoelectric point (pI)?

300

Keratin is this type of protein.

What is a fibrous protein?

400

These types of bonds stabilize higher-level protein structures.

What are non-covalent interactions and forces?

400

These amino acids will "hide" inside proteins to avoid water.

What are hydrophobic amino acids?

400

The structure with a phi angle of -57 degrees and a psi angle of -47 degrees.

What is an alpha-helix?

400

This group will be deprotonated first in amino acids and its pKa is labeled as pKa1.

What is the carboxylic acid group?

400

This is a part of a polypeptide chain that is independently stable and can move as a single entity.

What is a domain?

500

The description of quaternary structures.

What is the arrangement of 2+ separate polypeptide chains in 3-dimensional complexes?

500

The amino acids in the polypeptide VEKA in order. Double Points if drawn!

What is Valine, Glutamate, Lysine, and Alanine?

500

Ramachandran plots show this and aid in predicting this (2 parts).

What are the values of the torsional angles and prediction of the protein/amino-acid conformation?

500

The determination of how many pKas an amino acid will have on a titration curve.

What is the number of groups that will readily be deprotonated in increased pH?

500

The rule that determines hydrogen bonding in an a-helix and the groups involved (2 parts, tell me the rule and the groups involved in the bonding).

What is the n+4 rule in which the oxygen of a main chain carboxyl group will hydrogen bond the hydrogen of a main chain amino group 4 residues ahead?

M
e
n
u