Biochem Protein Lecture 1 Flashcards
Proteins are polymers of
Amino Acids
Each amino acid residue is joined to its neighbor by a specific type of covalent bond:
Peptide Bond
How many different amino acids are commonly found in proteins?
Are there many less common ones?
20
Yes
What does each amino acid have?
The amino acids differ from each other in their
1) A carboxylic acid group
2) An amino group bonded to the same carbon atom (α carbon)
Side Chains (R-groups
Amino acids are grouped into 5 main classes based on their
R-Group Properties
Which R-Group property of AAs is particularly important?
Polarity
AAs vary from nonpolar and hydrophobic to polar and hydrophilic
This amino acid is the simplest structure of the aliphatic non-polar R-group.
Glycine
These nonpolar, alkyl groups tend to cluster together within proteins and stabilize proteins through hydrophobic interactions
Alanine, Valine, Leucine, and isoleucine
This amino acid is a non-polar aliphatic and is one of two sulfur containing AAs and has a nonpolar thioether group in its side chain. Note that the electronegativity of sulfur is similar to carbon
Methionine
This AA has nonpolar aliphatic side chain with cyclic structure; it’s secondary amino (imino) group is held in rigid conformation, which reduces flexibility of polypeptides containing proline
Proline
T/F: Aromatic R groups are relatively nonpolar and hydrophobic
TRUUUUUEEEE
This is the 1st aromatic R group
Phenylalanine
This aromatic R-Group has a bicyclic ring (indole), it contains an NH group which can form H bonds
Tryptophan
This aromatic R-group contains an OH group which can H-bond
Tyrosine
Why are tyrosine and tryptophan more polar than phenylalanine?
Because of their H-bonding ability
All aromatic aa’s absorb UV light, especially
What absorbance is characteristic of most proteins?
tryptophan
280nm