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The tertiary structure of a protein is primarily responsible for:

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Explanation

The context explains: 'The tertiary structure of proteins represents overall folding of the polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular shapes viz. fibrous and globular.' and 'Tertiary structure is absolutely necessary for the many biological activities of proteins.'

What kind of forces are primarily responsible for stabilizing the secondary and tertiary structures of proteins?

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Explanation

The context details: 'The main forces which stabilize the 2° and 3° structures of proteins are hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.'

Which of the following is an example of a globular protein mentioned in the text?

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Explanation

The context provides: 'Globular proteins... Insulin and albumins are the common examples of globular proteins.'

Adult human haemoglobin is described as having a quaternary structure. This means it is an assembly of:

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Explanation

The context states: 'Some proteins are an assembly of more than one polypeptide or subunits. The manner in which these individual folded polypeptides or subunits are arranged with respect to each other... is the architecture of a protein otherwise called the quaternary structure of a protein. Adult human haemoglobin consists of 4 subunits.'

If a protein loses its biological activity due to changes in temperature or pH, it is undergoing:

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Explanation

The context explains: 'When a protein in its native form, is subjected to physical change like change in temperature or chemical change like change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This is called denaturation of Proteins.'

Enzymes, being proteins, possess which of the following structural levels?

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Explanation

The context implies all levels. It states: 'An enzyme like any protein has a primary structure, i.e., amino acid sequence of the protein. An enzyme like any protein has the secondary and the tertiary structure.' And since some enzymes are multi-subunit, they would also have quaternary structure, similar to other proteins described (e.g., hemoglobin).

The overall folding of the polypeptide chains, leading to fibrous or globular shapes, is characteristic of which protein structure level?

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Explanation

The chemistry context states: 'The tertiary structure of proteins represents overall folding of the polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular shapes viz. fibrous and globular.'

Which statement best differentiates between secondary and tertiary protein structures?

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Explanation

The context defines secondary structure as 'regular folding of the backbone... two different types of structures viz. $\alpha$-helix and $\beta$-pleated sheet structure' and tertiary structure as 'overall folding of the polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular shapes viz. fibrous and globular.'

In the quaternary structure of adult human haemoglobin, how many subunits are involved and what are their types?

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Explanation

The context states: 'Adult human haemoglobin consists of 4 subunits. Two of these are identical to each other. Hence, two subunits of $\alpha$ type and two subunits of $\beta$ type together constitute the human haemoglobin (Hb).'

A 'native protein' is described as having a unique three-dimensional structure and biological activity. Which level(s) of protein structure are essential for a protein to exhibit its biological activity in its native form?

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Explanation

The context implies that all higher-order structures (secondary, tertiary, and quaternary) are built upon the primary structure. The tertiary structure is stated to be 'absolutely necessary for the many biological activities,' and the quaternary structure is also involved in the function of multi-subunit proteins like hemoglobin. Therefore, for a protein to function in its 'native form,' all its structural levels are essential.

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