Alpha helices and beta sheets are examples of----- protein organization.
A.Primary structure
B.Secondary structure
C.Tertiary structure
D.Quaternary structure
Answer
Verified
460.5k+ views
Hint: Proteins are the large biomolecules, which consists of one or more long chains of amino acid residues. Proteins perform different functions like metabolic reactions, DNA replication, responding to stimuli, transporting molecules. etc based on their shapes. The proteins get the final shape based on the four levels of protein structure.
Complete answer:
Here, the distinct structures of protein organisation have been classified into- primary structure, secondary structure, tertiary structure, and quaternary structure. The secondary structure, which forms within a polypeptide due to interaction between atoms of the backbone and that usually refers to local folded structures.
The most common type of secondary structure here is Alpha helix and beta-pleated sheet. They are held in a shape by hydrogen bonds. They form between the carbonyl O of one amino acid and the amino H of another. In Alpha helix, the carbonyl of one amino acid is hydrogen bonded to the amino H of an amino acid.
The pattern of bonding of the Alpha helix resembles a curled ribbon like structure. In the Beta pleated sheet, when two or more segments of polypeptides chain line up next to each other, they form a sheet-like structure by holding the hydrogen bonds together. The strands present here may be parallel(pointing the same direction) or anti-parallel (pointing opposite direction).
Hence the correct answer is OPTION(B)
Note: Many proteins contain both Alpha helices and Beta sheets, even though some contain just one type of secondary structure. If the temperature of a protein environment is changed or when it is exposed to chemicals, they denatured. They will lose their three-dimensional structure and they are non-functional.
Complete answer:
Here, the distinct structures of protein organisation have been classified into- primary structure, secondary structure, tertiary structure, and quaternary structure. The secondary structure, which forms within a polypeptide due to interaction between atoms of the backbone and that usually refers to local folded structures.
The most common type of secondary structure here is Alpha helix and beta-pleated sheet. They are held in a shape by hydrogen bonds. They form between the carbonyl O of one amino acid and the amino H of another. In Alpha helix, the carbonyl of one amino acid is hydrogen bonded to the amino H of an amino acid.
The pattern of bonding of the Alpha helix resembles a curled ribbon like structure. In the Beta pleated sheet, when two or more segments of polypeptides chain line up next to each other, they form a sheet-like structure by holding the hydrogen bonds together. The strands present here may be parallel(pointing the same direction) or anti-parallel (pointing opposite direction).
Hence the correct answer is OPTION(B)
Note: Many proteins contain both Alpha helices and Beta sheets, even though some contain just one type of secondary structure. If the temperature of a protein environment is changed or when it is exposed to chemicals, they denatured. They will lose their three-dimensional structure and they are non-functional.
Recently Updated Pages
One difference between a Formal Letter and an informal class null english null
Can anyone list 10 advantages and disadvantages of friction
What are the Components of Financial System?
How do you arrange NH4 + BF3 H2O C2H2 in increasing class 11 chemistry CBSE
Is H mCT and q mCT the same thing If so which is more class 11 chemistry CBSE
What are the possible quantum number for the last outermost class 11 chemistry CBSE
Trending doubts
10 examples of friction in our daily life
Difference Between Prokaryotic Cells and Eukaryotic Cells
What is the specific heat capacity of ice water and class 11 physics CBSE
One Metric ton is equal to kg A 10000 B 1000 C 100 class 11 physics CBSE
State and prove Bernoullis theorem class 11 physics CBSE
State the laws of reflection of light