EPSPS is an enzyme used by plants to catalyze the production of the amino acids
ID: 280534 • Letter: E
Question
EPSPS is an enzyme used by plants to catalyze the production of the amino acids tyrosine, tryptophan and phenylalanine. Round-up kills plants by entering cells, binding to this enzyme and preventing the formation of these essential amino acids, and is thought to be safe for humans and other animals. The EPSPS enzyme is a protein that has primary, secondary and tertiary structure What is meant by primary, secondary and tertiary structure? A complete answer will include the type of bonds/forces/interactions that cause the protein to form each level of structure.Explanation / Answer
Hi Answer:
Answer: Proteins are made up of amino acids or we can say that the polymer of the amino acid is known as proteins. Proteins exist in 4 different kinds of the structure according to their folding, bonding and confirmations. These structures are Primary, Secondary, Tertiary and Quaternary structure. Presently the enzyme EPSPS exists in three structures i.e. Primary, Secondary, and Tertiary, which are explained in details in subsequent sections.
A. Primary structure: the linear structure or arrangement of amino acids is known as the primary structure of proteins. In this structure the amino terminal is known as N- terminal or carboxyl – terminal is known as C- terminal. In primary structure, amino acids are bound to each other by means of peptide bonds and form a long backbone structure having different amino acid side chains are producing from this. Depending on the amino acid present in a proteins primary structure we can distinguish whether the protein is acid, basic or neutral in nature.
B. Secondary structure: the secondary structure of a protein is generally a three-dimensional form of a local segment of protein. The secondary structure depends on the hydrogen bonding in the proteins. There are two types of secondary structure are present (alpha-helix and beta-sheet.)
(i) Alpha-helix is a right-handed coiled stand. The side chain subunits of the amino acids groups extended towards the outside in this type of structure. The formation of Hydrogen bonding took place between the oxygen of the C=O of each peptide bond present in the strand and the hydrogen atom of the N-H group of the peptide bond. Due to the presence of hydrogen bonding, this structure becomes stable.
(ii) Beta-sheets: In this type of secondary structure hydrogen bonding took place between the strands rather than the inside the strands. In this confirmation pair of strains lying side-by-side. There is hydrogen bonding between carbonyl oxygen of one strand with the amino hydrogens of the second strand. In present confirmation, two strands can exist in parallel or antiparallel directions. Due to the well-aligned hydrogen bonding present in anti-parallel beta sheets, they are more stable than parallel beta sheets.
C. Tertiary structure: The three-dimensional shape of the protein molecule is known as a tertiary structure of the protein. In this state, protein molecules twist or bends to make itself maximum stable. It is irregular and random state of protein structure. The disulfide bridge formation by the oxidation of the sulfhydryl groups on cysteine causes the stability or stabilization of protein tertiary structure. These bridges allowing different parts of the protein chain to be held together covalently. Additionally, hydrogen bonds may form between different side-chain groups. In additions to this, the ionic interactions between positively and negatively charged amino acids also play a role in stabilization of this structure.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.