Key Point Worksheets 1-3 Flashcards
Why is there a trans conformation for (R-) side groups on adjacent amino acids when forming the peptide?
Trans configuration decreases steric hindrance of R groups by keeping the side chains of adjacent amino acids farther apart, leading to a more stable and less crowded peptide structure.
What is a prosthetic group?
A non-protein molecule that is tightly & permanently bound to a protein and is needed for the protein’s biological activity. Typically involved in the protein’s function, often participating in the protein’s chemical reactions or helping stabilize the protein’s structure.
What forces or bonds stabilize the primary structures?
Peptide bonds.
Give the functional group of alcohol, ketone, carboxylic acid, aldehyde.
-OH; -C=O; -COOH; -CHO (double bond O)
Give the functional group of primary amine, thiol, ether, ester,
-NH2; -SH; -ROR; -RC=OO-R;
Give the functional group of amide, phosphate, & a compound that contains an acyl group.
O=C-NH2; PO4; -Cl-C=O Acteyl chloride
List the AAs that have hydrophobic side chains.
Glycine (Gly), alanine (Ala), Valine (Val), Leucine (Leu), Isoleucine (Ile), Proline (Pro), Phenylalanine (Phe), Methionine (Met) & Tryptophan (Trp)
List the AAs that have polar side chains.
Serine (Ser), Threonine (Thr), Cysteine (Cys), Asparagine (Asn), Glutamine (Gln) & Tryosine (Tyr)
All acidic or basic AAs are ______ AAs. All AAs can form ____ bonds.
polar; hydrogen
List the aliphatic AAs.
Glycine, alanine, valine, leucine, isoleucine, proline.
List the aromatic AAs.
Phenylalanine, tryosine, tryptophan
List the sulfur-containing AAs.
Cysteine, methionine.
List the alcohol-containing AAs.
Serine, threonine
List the basic AAs.
Histidine, lysine, Arginine
List the acidic AAs.
Asparate, glutamate, asparagine, glutamine.