The levels of structure found in proteins in order.
What is primary structure, secondary structure, tertiary structure, and quaternary structure?
The 4 main groups of amino acids.
What are non-polar (hydrophobic), polar, positively charged (basic), and negatively charged (acidic) amino acids?
These bonds are planar.
What are peptide bonds?
As pH increases, this happens to amino acids.
What is deprotonation?
These things can cause denaturation (5 parts will accept 3/5).
What are extreme pH changes, temperature, miscible organic solvents, detergents, and certain solvents?
Common secondary structures found in proteins (4 structures).
What are a-helices, B-sheets, B-turns, and random coils?
The bond that joins amino acids in a polypeptide.
What is a peptide bond?
Rotation is allowed around these bonds in a polypeptide.
What is the alpha-carbon/amino bond and the alpha-carbon/ carboxyl carbon bond?
At very low pHs (no OH added), amino acids will exist in this form.
What is fully protonated?
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?
Tertiary structure describes this property of proteins.
What is the well-defined, three-dimensional fold adopted by proteins?
The stereoisomer amino acids predominately exist in.
What is an L absolute configuration?
These are the names of the dihedral angles found in a polypeptide.
What are phi and psi?
The point at which amino acids have a net neutral charge on a titration curve.
What is the isoelectric point (pI)?
Keratin is this type of protein.
What is a fibrous protein?
These types of bonds stabilize higher-level protein structures.
What are non-covalent interactions and forces?
These amino acids will "hide" inside proteins to avoid water.
What are hydrophobic amino acids?
The structure with a phi angle of -57 degrees and a psi angle of -47 degrees.
What is an alpha-helix?
This group will be deprotonated first in amino acids and its pKa is labeled as pKa1.
What is the carboxylic acid group?
This is a part of a polypeptide chain that is independently stable and can move as a single entity.
What is a domain?
The description of quaternary structures.
What is the arrangement of 2+ separate polypeptide chains in 3-dimensional complexes?
The amino acids in the polypeptide VEKA in order. Double Points if drawn!
What is Valine, Glutamate, Lysine, and Alanine?
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?
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?
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?