Amino Acids Affect Protein Folding

Question 1

What about the R-group of amino acids affects protein folding?

Answer 1

Polarity/hydrophobicity

Question 2

What about the structures of tyrosine, phenylalanine, and tryptophan in particular influences their folding in a protein?

Answer 2

These amino acids contain aromatic side chains, making them particularly large. Tryptophan in particular is the bulkiest amino acid due to its double ring structure. The sheer size of these amino acids need to be accomodated during folding.

Question 3

What about the structure of glycine influences its folding in a protein?

Answer 3

Glycine is the smallest amino acid and gives protein a lot of structural flexibility.

Question 4

What about cysteine’s structure influences how it folds in a protein?

Answer 4

Two cysteine side chains can form disulfide bonds with one another.

Question 5

What about the structure of proline influences how it folds in a protein?

Answer 5

Proline is technically an imino acid. The side chain locks the bond between the backbone nitrogen and the alpha carbon, taking away a lot of structural flexibility in a protein.

Question 6

Is the backbone of proteins charged?

Answer 6

Yes, negatively charged.

Question 7

What non-covalent attractions influence protein folding?

Answer 7

Electrostatic attractions, hydrogen bonds, van der Waals interactions