Classify each protein example according to its highest level of protein structure.
When performing site-directed mutagenesis to test predictions about which residues are essential for protein function, wh amino acid substitution would disrupt protein structure the most.
Primary Structure
Amino acid sequence of myoglobin
Secondary Structure
the C-helix of a -lactalbumin
Tertiary Structure
A single hemoglobin subunit with heme
Quaternary Structure
Hemoglobin
Aminoacid sequences of a protein are generally called as their primary structure as they are primarily responsible for their entire structure. Hence the amino acid sequence of myoglobin is the primary structure.
The intermediate forms of a protein formed before they fold are their secondary structures. Alpha helix and beta pleated sheets are the most common secondary structures. Hence the C helix of alpha-lactalbumin is the secondary structure.
The tertiary structure of a protein is the structure of its single polypeptide chain with its secondary structures. Hence a single hemoglobin subunit with heme is it's tertiary structure.
Quaternary structure is the assemblage of multiple folded units of a protein into a multi-subunit complex. Hemoglobin is one of this kind of structures. Hence hemoglobin is a quaternary structure.
Classify each protein example according to its highest level of protein structure.
When performing site-directed mutagenesis to test predictions about which residues are essential for protein function, which amino acid substitution would disrupt protein structure the most.
1. You are performing mutagenesis to test predictions about which residues are essential for a protein's function. Which of the each pair of amino acid substitutions listed below would you expect to disrupt protein structure most and WHY? Val replaced by F or A Lys replaced by Asp or R Gln replaced by Glu or Asn Pro replaced by His or Gly
Classify each protein example according to its highest level of protein structure. Primary structure Secondary structure Tertiary structure Quaternary structure myoglobin with heme thethe C helix of α-lactalbumin Gly-Ala-Val-Leu hemoglobin
24. The _______ of amino acids in a protein is referred to as its primary structure. A) twisting B) sequencing C) folding D) none of these 25. The structure of a protein is most important because the _______ of the amino acids determines its overall shape, function and properties. A) primary, twisting B) primary, sequencing C) secondary, twisting D) secondary, folding E) none of these 26. The secondary structure of a protein is due to_______ between amino acid residues. A) hydrophobic interactions B) hydrogen bonding...
What is the highest level of protein structure in each of the protein examples below? Move each example to the correct classification.
What is the highest level of protein structure in each of the
protein examples below? Move each example to the correct
classification.
Fully describe and illustrate each level of protein structure. What type(s) of chemical bond/interactions are essential at each level? When heat or a strong acid/base is applied, which level of protein structure is least affected?
11.Which of the following mutations would most likely to disrupt the structure of an α-helix? Cys to Ala Lys to Arg Glu to Gly Val to Leu 12.Which amino acid combination is the most preferred to occupy positions 1 and 4 in an α-helix? Glu and Lys Phe and Pro Lys and Arg Asp and Glu 13.If each turn in the standard alpha helix extends 5.4 A and there are 3.6 amino acid residues per turn, how many amino acids...
6.) Provide short answers for the questions about protein structure below: a.) True or False, amino acid sequence defines the native structure of protein. b.) What is the main type of bonding responsible for stabilizing the secondary structure of proteins? c.) Briefly discuss the thermodynamics of protein folding into its native 3D structure. Is this process enthalpy driven or entropy driven? d.) Give an example of 2 major secondary structural motifs found in polypeptides. Do any of these motifs appear...
can
you just answer 1,3,4 then ?
All of 20 hing Med ia 1 The incide d together by chemical beads to form long chains, in the same way that ar e made of long chains of simple molecules Unlike carboidrates, however, protein molecules fold pinc h pes are for their higical function. The folded structure of a protein depends on the sequence of the amino acid building block that forms the polymer chain. A folded protein is shown on...