Hey guys!
I think for 13 the answer is Amonium Sulfate cuz its cheap and the third one is cysteien cuz u get the S-S bonds?
13. To concentrate an enzyme without denaturing it, you would likely use...
urea ammonium sulfate a detergent HCl NaOH PITC
14. The tertiary strucure of many proteins is stabilized by covalent bonds between the side chains of
Asn Met Pro Cys Ser Trp
15. To find the answer for question 13, we need to understand the purpose of each option given.
- Urea is a chemical compound commonly used as a denaturant, meaning it can disrupt the structure of proteins. Therefore, it is not a suitable choice for concentrating enzymes without denaturing them.
- Ammonium sulfate is often utilized for protein precipitation or salting out. It helps to separate proteins from other components in a solution, making it a good choice to concentrate enzymes without denaturing them.
- A detergent is typically used to solubilize proteins and disrupt lipid membranes. It may not be the most appropriate option for concentrating an enzyme without denaturing it.
- HCl (hydrochloric acid) and NaOH (sodium hydroxide) are strong acids and bases, respectively. They are unlikely to be used to concentrate enzymes without denaturing them as they can have damaging effects on proteins.
- PITC (phenylisothiocyanate) is often used in protein sequencing but is not typically employed for the concentration of proteins.
Therefore, considering the given options, ammonium sulfate appears to be the most suitable choice for concentrating an enzyme without denaturing it.
16. To find the answer for question 14, we need to consider which amino acid side chains can form covalent bonds to stabilize the tertiary structure of proteins.
- Asparagine (Asn) does not typically form covalent bonds between its side chains.
- Methionine (Met) has a sulfur-containing side chain, but it does not typically participate in covalent bonding for tertiary structure stabilization.
- Proline (Pro) has a unique structure that does not readily form covalent bonds for tertiary stabilization.
- Cysteine (Cys) does form covalent bonds with other cysteine residues, specifically disulfide bonds (S-S bonds). These disulfide bonds can be important for stabilizing the tertiary structure of proteins.
- Serine (Ser), although it has a hydroxyl group, does not typically participate in the formation of covalent bonds for tertiary structure stabilization.
- Tryptophan (Trp) also does not typically participate in the formation of covalent bonds for tertiary structure stabilization.
Based on this information, the correct answer would be Cysteine (Cys) since it can form covalent bonds, specifically disulfide bonds (S-S bonds), between its side chains to stabilize the tertiary structure of proteins.