Advertisements
Advertisements
Question
Write one difference between α-helix and β-pleated structures of proteins.
Advertisements
Solution
| α -helix | β -pleated sheet |
| The α -helix results from coiling of the protein chain such that the peptide bonds making up the backbone are able to form hydrogen bonds between each other. | The β -pleated sheet is a layering of protein chains one on the top of another. |
APPEARS IN
RELATED QUESTIONS
What type of bonding helps in stabilising the α-helix structure of proteins?
The correct statement for protein haemoglobin.
α-Helix is a secondary structure of proteins formed by twisting of polypeptide chain into right-handed screw like structures. Which type of interactions are responsible for making the α-helix structure stable?
Which moieties of nucleosides are involved in the formation of phosphodiester linkages present in dinucleotides? What does the word diester in the name of linkage indicate? Which acid is involved in the formation of this linkage?
Assertion: β-glycosidic linkage is present in maltose,
Reason: Maltose is composed of two glucose units in which C–1 of one glucose unit is linked to C–4 of another glucose unit.
Explain the terms primary and secondary structure of proteins. What is the difference between α-helix and β-pleated sheet structure of proteins?
Explain formation of peptide linkage in protein with an example.
Out of the following, which type of interaction is responsible for the stabilisation of the α-helix structure of proteins?
The total number of negative charge in the tetrapeptide, Gly-Glu-Asp-Tyr at pH 12.5 will be ______. (Integer answers)
Statement I: A protein is imagined as a line, the left end represented by first amino acid (C-terminal) and the right end represented by last amino acid (Nterminal).
Statement II: Adult human haemoglobin, consists of 4 subunits (two subunits of a type and two subunits β type.)
In the light of the above statements, choose the correct answer from the options given below:
