26. Primary and secondary bonds in proteins, their roles in 3D-structure stabilization. Cooperativity, folding, dynamics in protein function.

Question 1

What is Conformation?

Answer 1

orientations of peptide bonds

Question 2

2 possible peptide structures

Answer 2

Alpha helix and beta sheets

Question 3

Interactions stabilizing 3D structure of proteins

Answer 3

Question 4

What is Cooperativity?

Answer 4

many secondary interactions (bonds) keep and connect together the 3D-structures of proteins

Question 5

Describe primary bond of protein

Answer 5

The primary structure of a protein consists of amino acids chained to each other. Amino acids are joined by peptide bonds. A peptide bond is a type of covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid.

Question 6

Describe secondary bonds in protein

Answer 6

Secondary structure refers to regular, recurring arrangements in space of adjacent amino acid residues in a polypeptide chain. It is maintained by hydrogen bonds between amide hydrogens and carbonyl oxygens of the peptide backbone.

Question 7

Protein folding

Answer 7

process by which a polypeptide chain folds to become a biologically active protein in its native 3D structure.

Question 8

What is Levinthal’s paradox?

Answer 8

Levinthal’s paradox is that finding the native folded state of a protein by a random search among all possible configurations can take an enormously long time

50% folding: half of the proteins are folded, the other half is unfolded!

Question 9

What is Protein dynamics ~ flexibility?

Answer 9

a highly complex phenomenon comprising numerous contributions from motions with different mechanisms of action and happening with diverse timescales and amplitudes that highly depend on the system and the local environment.