b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.

The peptide bond is a stronger bond than the ester bond. What structural feature of the peptide bond gives it additional bond strength?

Which of the following most directly applies to the formation of the secondary structures of proteins? A B с D formation of ionic bonds between the R groups of two polypeptides formation of nonpolar interactions between two R groups on the same polypeptide formation of covalent bonds via dehydration reactions between two amino acids formation of hydrogen bonds between between amino and carboxyl groups

Select A letter for each part

Refer to the structure of an oligopeptide below: OH но. NH SH Taking note of the component residues, would such a structure as it is drawn above be possible at any pH value? (Yes or No)?

Having peptides arranged in a beta sheet would be an example of a secondary structure A) True B) False

Draw the structure of Lys and Ala linked by an isopeptide bond.

The following figure is a diagram (cartoon or caricature) of the structure of a protein. What types of secondary structure are observed in the molecule? Is it a globular protein or a fibrous one?

Disulfide bonds help to stabilize the three-dimensional structure of proteins. What amino acids are involved in the formation of disulfide bonds? Does the formation of a disulfide bond increase or decrease entropy (ΔS)?

What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.