The effect of base-pair substitution mutations on protein function varies widely from no detectable effect to the complete loss of a protein function. Why the functional consequences of base-pair substitution vary so widely?

The effect of base-pair substitution mutations on protein function varies widely from no detectable effect to the complete loss of a protein function. Why the functional consequences of base-pair substitution vary so widely?

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Description: The effect of base-pair substitution mutations on protein function varies widely from no detectable effect to the complete loss of a protein function. Why the functional consequences of base-pair substitution vary so widely?

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter21: Dna, Genes, And Biotechnology

Section: Chapter Questions

Problem 2RQ

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Similar questions

Some mutations affect changes in protein structure and function that can result in disease whereas other mutations have no significant effects on protein structure and function. Please explain reasons for the above mentioned statement
What is the resulting polypeptide: _______________________________________________________? What effect does this mutation have on the polypeptide? Make sure to compare to the original polypeptide. What effect might this have on the function of the protein? Why?
Why would the mutation Ile -> Asp be likely to destabilize a protein? Why would the mutation Ile ->Val be likely to destabilize a protein? Why would the mutation Val -> Ile be likely to destabilize a protein?
What is the resulting polypeptide: _______________________________________________________? What effect does this mutation have on the polypeptide? Make sure to compare to the original polypeptide. Would this mutation allow the protein for perform the intended function? Why or why not?
When an inappropriate amino acid is substituted in place of another, as occurs in certain genetic disorders, the resulting protein is either poorly functional or non-functional. Since proteins contain hundreds if not thousands of amino acids, why should the change of a single amino acid be so critical?
The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?
Some substitution mutation result in a malfunctioning protein but others do not. Why is this?
How would a substitution mutation in the third nucleotide position of the codons for alanine and valine affect the resulting protein?
A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutantpolypeptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?) (Hint: Photocopy the fingerprints, cut them out, and overlay them.)
Why do some genetic mutations lead to completely nonfunctional proteins while others do not affect the functioning of the resulting protein at all?
Why is selenocysteine called the 21st amino acid when there are many more amino acids found than the 20 basic ones coded for by the genetic code?
In protein analysis, these macromolecules need different correction factors because they have different amino acid sequences True or False?