Question

In: Biology

1. What non-covalent interactions can (1) Alanine and (2) Threonine acid participate in, as part of...

1. What non-covalent interactions can (1) Alanine and (2) Threonine acid participate in, as part of tertiary structure at pH 7? Include an explanation of the charges involved (full or partial, permanent or temporary)?

2. Suggest one amino acid whose side chain can participate in a non-covalent interaction with the side chain of alanine, and one amino acid whose side chain can participate in a non-covalent interaction with the side chain of threonine.

Solutions

Expert Solution

The structures of alanine and threonine in proteins are as above.

1.From above it is clear that side chain of alanine is simply methyl group ( -CH3 ) This group is non-polar thus it will participate in tertiary structure through non-covalent hydrophobic interaction.

From above it is clear that the side chain of Threonine contains hydroxyl (-OH) group. This group is polar in nature in which hydrogen atom carries permanent, partial, positive charge and oxygen atom carries permanent, partial, negative charge. Thus this group has the ability to form Hydrogen Bond.  Thus it will participate in tertiary structure through non-covalent Hydrogen-Bonding.

Since the side chain of alanine is non-polar it will interact non-covalently with the amino acid which has non-polar side chain like valine, leucine, isoleucine, etc.

Similarly threonine will interact non-covalently with amino acids serine, tyrosine, etc which have polar uncharged side chains due to presence of hydroxyl (-OH) group in their side chain.


Related Solutions

What type of interactions are important and prevalent in biological systems? Non-covalent or Covalent? Please explain...
What type of interactions are important and prevalent in biological systems? Non-covalent or Covalent? Please explain your choice. Can you provide examples of both these types of interactions in the context of protein structure that you learned.
1.Why are non-covalent bonds important in biological systems? List at least three examples of non-covalent interactions....
1.Why are non-covalent bonds important in biological systems? List at least three examples of non-covalent interactions. 2. You want to amplify at least the underlined sequence, you can have some flanking sequence as well.       5’CTGCTACGTACTGGATGACTGACTGTGATGATCTGATCCCAGTGCTCGTAGTCGTGCGTTCGTAATATATAGCGATGGCGCGATGCGATGCGCGTAGCGGCTAGGCGTAGGCGGATTCGGCTAGGCGATGGCGATGGCGATGCGATATTCTAGCGCTAGCGATGAGGTGATTATATCGGCGCTAGCTGATCGTAGCTGATCG 3’ Design the most optimal primers according to Tm and length. Write out each primer and show which is the 5’ and 3’ end of each primer. How big will your PCR product be? 3.. What are the differences between covalent bonds and non-covalent...
describe the chemical nature of the non-covalent bonding interactions between peptides and lipids.
describe the chemical nature of the non-covalent bonding interactions between peptides and lipids.
In the following diagram, solid lines represent covalent bonds while dotted lines represent non-covalent interactions. Which...
In the following diagram, solid lines represent covalent bonds while dotted lines represent non-covalent interactions. Which of the depictions of molecules show a hydrogen bonding interaction. Check all systems that apply. Consult Textbook Your Answers:      H—H —N‧‧‧‧‧H—O— —C‧‧‧‧‧H—F— —O‧‧‧‧‧H—C— Submit Feedback: Question 14 Identify which of the following molecules have a net dipole moment: Consult Textbook Your Answers: CCl4 CH2Cl2 (CH3)2O CO2 BF3 Submit Feedback: Question 15 Determine the predominant intermolecular force in each of the following substances: Consult Textbook...
Name and thoroughly discuss the 4 non-covalent interactions that are responsible for stabilizing the secondary structures...
Name and thoroughly discuss the 4 non-covalent interactions that are responsible for stabilizing the secondary structures of proteins?
1.)  Part of the amino acid sequence of the A chain of insulin is "glutamine-cysteine-cysteine-alanine". Which of...
1.)  Part of the amino acid sequence of the A chain of insulin is "glutamine-cysteine-cysteine-alanine". Which of the following DNA strands could encode this peptide? A. 5'-CCCCCGCAGAAG-3' B. 5'-GGCATCGTGGAG-3' C. 5'-CTGCCCCGACAC-3' D. 5'-CAGTGCTGTGCC-3' E. 5'-GTCACGACACGG-3' Explain how you determined the answer. 2.) Arrange the following genetic terms in order of complexity from largest to smallest. 1. chromosome 2. nucleotide 3. genome 4. double helix 3.) Using the following template strand of DNA, what would be the translation? 5’ TACCGTACT 3’ 4.)  Using...
Using your knowledge of the main types of non-covalent interactions that occur in biological chemistry, discuss...
Using your knowledge of the main types of non-covalent interactions that occur in biological chemistry, discuss the spontaneous assembly of the four main types of biological structure with stable structures: DNA, proteins, glycans (such as cellulose and chitin) and cell membranes. Compare and contrast the various structures in terms of the forces and chemical structures driving their assembly. Finally, discuss why their particular molecular structures allow them to perform their biological roles.
1.What is the name for the covalent bonds that create the Nucleic Acid backbone? 2.Define Complementarity...
1.What is the name for the covalent bonds that create the Nucleic Acid backbone? 2.Define Complementarity as it is used in nucleic acid base pairing and explain how complimentary base pairing is the basis for making faithful copies of DNA from DNA templates and RNA from DNA templates.
Which are true and which are false? a)The molecule CH3CH2CH2CH3 can participate in hydrophobic interactions.
Which are true and which are false? and why is that the answer a)The molecule CH3CH2CH2CH3 can participate in hydrophobic interactions. b)Strong bonds are important in biochemistry because enzymes cannot break strong bonds c)ATP hydrolysis can be coupled with non-spontaneous reactions to make them spontaneous
Part A: Zwitterionic Form Two structures of alanine can be drawn that have a net charge...
Part A: Zwitterionic Form Two structures of alanine can be drawn that have a net charge of zero, but the predominant form of alanine at its pI is zwitterionic. Why is alanine predominantly zwitterionic rather than completely uncharged at its pI? What percent (to one significant figure) of alanine molecules would be in the completely uncharged form at the pI? Hint: pK1 of alanine is 2.35 and pK2 is 9.87. (answer is NOT .24%) Part B: Hardy-Weinberg The following question...
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT