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1 | 7705-7708 | 2
10 2
10 2
10 2
10 |
1 | 7706-7709 | 2
10 2
10 2
10 2
Proteins
Proteins
Proteins
Proteins
Proteins
Rationalised 2023-24
291
Biomolecules
5 |
1 | 7707-7710 | 2
10 2
10 2
Proteins
Proteins
Proteins
Proteins
Proteins
Rationalised 2023-24
291
Biomolecules
5 Isoleucine*
H3C-CH2-CH-
Ile
I
|
CH3
6 |
1 | 7708-7711 | 2
10 2
Proteins
Proteins
Proteins
Proteins
Proteins
Rationalised 2023-24
291
Biomolecules
5 Isoleucine*
H3C-CH2-CH-
Ile
I
|
CH3
6 Arginine*
HN=C-NH-(CH2)3-
Arg
R
|
NH2
7 |
1 | 7709-7712 | 2
Proteins
Proteins
Proteins
Proteins
Proteins
Rationalised 2023-24
291
Biomolecules
5 Isoleucine*
H3C-CH2-CH-
Ile
I
|
CH3
6 Arginine*
HN=C-NH-(CH2)3-
Arg
R
|
NH2
7 Lysine*
H2N-(CH2)4-
Lys
K
8 |
1 | 7710-7713 | Isoleucine*
H3C-CH2-CH-
Ile
I
|
CH3
6 Arginine*
HN=C-NH-(CH2)3-
Arg
R
|
NH2
7 Lysine*
H2N-(CH2)4-
Lys
K
8 Glutamic acid
HOOC-CH2-CH2-
Glu
E
9 |
1 | 7711-7714 | Arginine*
HN=C-NH-(CH2)3-
Arg
R
|
NH2
7 Lysine*
H2N-(CH2)4-
Lys
K
8 Glutamic acid
HOOC-CH2-CH2-
Glu
E
9 Aspartic acid
HOOC-CH2-
Asp
D
O
||
10 |
1 | 7712-7715 | Lysine*
H2N-(CH2)4-
Lys
K
8 Glutamic acid
HOOC-CH2-CH2-
Glu
E
9 Aspartic acid
HOOC-CH2-
Asp
D
O
||
10 Glutamine
H2N-C-CH2-CH2-
Gln
Q
O
||
11 |
1 | 7713-7716 | Glutamic acid
HOOC-CH2-CH2-
Glu
E
9 Aspartic acid
HOOC-CH2-
Asp
D
O
||
10 Glutamine
H2N-C-CH2-CH2-
Gln
Q
O
||
11 Asparagine
H2N-C-CH2-
Asn
N
12 |
1 | 7714-7717 | Aspartic acid
HOOC-CH2-
Asp
D
O
||
10 Glutamine
H2N-C-CH2-CH2-
Gln
Q
O
||
11 Asparagine
H2N-C-CH2-
Asn
N
12 Threonine*
H3C-CHOH-
Thr
T
13 |
1 | 7715-7718 | Glutamine
H2N-C-CH2-CH2-
Gln
Q
O
||
11 Asparagine
H2N-C-CH2-
Asn
N
12 Threonine*
H3C-CHOH-
Thr
T
13 Serine
HO-CH2-
Ser
S
14 |
1 | 7716-7719 | Asparagine
H2N-C-CH2-
Asn
N
12 Threonine*
H3C-CHOH-
Thr
T
13 Serine
HO-CH2-
Ser
S
14 Cysteine
HS-CH2-
Cys
C
15 |
1 | 7717-7720 | Threonine*
H3C-CHOH-
Thr
T
13 Serine
HO-CH2-
Ser
S
14 Cysteine
HS-CH2-
Cys
C
15 Methionine*
H3C-S-CH2-CH2-
Met
M
16 |
1 | 7718-7721 | Serine
HO-CH2-
Ser
S
14 Cysteine
HS-CH2-
Cys
C
15 Methionine*
H3C-S-CH2-CH2-
Met
M
16 Phenylalanine*
C6H5-CH2-
Phe
F
17 |
1 | 7719-7722 | Cysteine
HS-CH2-
Cys
C
15 Methionine*
H3C-S-CH2-CH2-
Met
M
16 Phenylalanine*
C6H5-CH2-
Phe
F
17 Tyrosine
(p)HO-C6H4-CH2-
Tyr
Y
18 |
1 | 7720-7723 | Methionine*
H3C-S-CH2-CH2-
Met
M
16 Phenylalanine*
C6H5-CH2-
Phe
F
17 Tyrosine
(p)HO-C6H4-CH2-
Tyr
Y
18 Tryptophan*
–CH2
N
H
Trp
W
19 |
1 | 7721-7724 | Phenylalanine*
C6H5-CH2-
Phe
F
17 Tyrosine
(p)HO-C6H4-CH2-
Tyr
Y
18 Tryptophan*
–CH2
N
H
Trp
W
19 Histidine*
His
H
20 |
1 | 7722-7725 | Tyrosine
(p)HO-C6H4-CH2-
Tyr
Y
18 Tryptophan*
–CH2
N
H
Trp
W
19 Histidine*
His
H
20 Proline
Pro
P
* essential amino acid, a = entire structure
Amino acids are classified as acidic, basic or neutral depending upon
the relative number of amino and carboxyl groups in their molecule |
1 | 7723-7726 | Tryptophan*
–CH2
N
H
Trp
W
19 Histidine*
His
H
20 Proline
Pro
P
* essential amino acid, a = entire structure
Amino acids are classified as acidic, basic or neutral depending upon
the relative number of amino and carboxyl groups in their molecule Equal number of amino and carboxyl groups makes it neutral; more
number of amino than carboxyl groups makes it basic and more
carboxyl groups as compared to amino groups makes it acidic |
1 | 7724-7727 | Histidine*
His
H
20 Proline
Pro
P
* essential amino acid, a = entire structure
Amino acids are classified as acidic, basic or neutral depending upon
the relative number of amino and carboxyl groups in their molecule Equal number of amino and carboxyl groups makes it neutral; more
number of amino than carboxyl groups makes it basic and more
carboxyl groups as compared to amino groups makes it acidic The
amino acids, which can be synthesised in the body, are known as non-
essential amino acids |
1 | 7725-7728 | Proline
Pro
P
* essential amino acid, a = entire structure
Amino acids are classified as acidic, basic or neutral depending upon
the relative number of amino and carboxyl groups in their molecule Equal number of amino and carboxyl groups makes it neutral; more
number of amino than carboxyl groups makes it basic and more
carboxyl groups as compared to amino groups makes it acidic The
amino acids, which can be synthesised in the body, are known as non-
essential amino acids On the other hand, those which cannot be
synthesised in the body and must be obtained through diet, are known
as essential amino acids (marked with asterisk in Table 10 |
1 | 7726-7729 | Equal number of amino and carboxyl groups makes it neutral; more
number of amino than carboxyl groups makes it basic and more
carboxyl groups as compared to amino groups makes it acidic The
amino acids, which can be synthesised in the body, are known as non-
essential amino acids On the other hand, those which cannot be
synthesised in the body and must be obtained through diet, are known
as essential amino acids (marked with asterisk in Table 10 2) |
1 | 7727-7730 | The
amino acids, which can be synthesised in the body, are known as non-
essential amino acids On the other hand, those which cannot be
synthesised in the body and must be obtained through diet, are known
as essential amino acids (marked with asterisk in Table 10 2) 10 |
1 | 7728-7731 | On the other hand, those which cannot be
synthesised in the body and must be obtained through diet, are known
as essential amino acids (marked with asterisk in Table 10 2) 10 2 |
1 | 7729-7732 | 2) 10 2 2
Classification of
Amino Acids
Rationalised 2023-24
292
Chemistry
Amino acids are usually colourless, crystalline solids |
1 | 7730-7733 | 10 2 2
Classification of
Amino Acids
Rationalised 2023-24
292
Chemistry
Amino acids are usually colourless, crystalline solids These are
water-soluble, high melting solids and behave like salts rather than
simple amines or carboxylic acids |
1 | 7731-7734 | 2 2
Classification of
Amino Acids
Rationalised 2023-24
292
Chemistry
Amino acids are usually colourless, crystalline solids These are
water-soluble, high melting solids and behave like salts rather than
simple amines or carboxylic acids This behaviour is due to the presence
of both acidic (carboxyl group) and basic (amino
group) groups in the same molecule |
1 | 7732-7735 | 2
Classification of
Amino Acids
Rationalised 2023-24
292
Chemistry
Amino acids are usually colourless, crystalline solids These are
water-soluble, high melting solids and behave like salts rather than
simple amines or carboxylic acids This behaviour is due to the presence
of both acidic (carboxyl group) and basic (amino
group) groups in the same molecule In aqueous
solution, the carboxyl group can lose a proton
and amino group can accept a proton, giving rise
to a dipolar ion known as zwitter ion |
1 | 7733-7736 | These are
water-soluble, high melting solids and behave like salts rather than
simple amines or carboxylic acids This behaviour is due to the presence
of both acidic (carboxyl group) and basic (amino
group) groups in the same molecule In aqueous
solution, the carboxyl group can lose a proton
and amino group can accept a proton, giving rise
to a dipolar ion known as zwitter ion This is
neutral but contains both positive and negative
charges |
1 | 7734-7737 | This behaviour is due to the presence
of both acidic (carboxyl group) and basic (amino
group) groups in the same molecule In aqueous
solution, the carboxyl group can lose a proton
and amino group can accept a proton, giving rise
to a dipolar ion known as zwitter ion This is
neutral but contains both positive and negative
charges In zwitter ionic form, amino acids show amphoteric behaviour as
they react both with acids and bases |
1 | 7735-7738 | In aqueous
solution, the carboxyl group can lose a proton
and amino group can accept a proton, giving rise
to a dipolar ion known as zwitter ion This is
neutral but contains both positive and negative
charges In zwitter ionic form, amino acids show amphoteric behaviour as
they react both with acids and bases Except glycine, all other naturally occurring a-amino acids are
optically active, since the a-carbon atom is asymmetric |
1 | 7736-7739 | This is
neutral but contains both positive and negative
charges In zwitter ionic form, amino acids show amphoteric behaviour as
they react both with acids and bases Except glycine, all other naturally occurring a-amino acids are
optically active, since the a-carbon atom is asymmetric These exist
both in ‘D’ and ‘L’ forms |
1 | 7737-7740 | In zwitter ionic form, amino acids show amphoteric behaviour as
they react both with acids and bases Except glycine, all other naturally occurring a-amino acids are
optically active, since the a-carbon atom is asymmetric These exist
both in ‘D’ and ‘L’ forms Most naturally occurring amino acids have
L-configuration |
1 | 7738-7741 | Except glycine, all other naturally occurring a-amino acids are
optically active, since the a-carbon atom is asymmetric These exist
both in ‘D’ and ‘L’ forms Most naturally occurring amino acids have
L-configuration L-Aminoacids are represented by writing the –NH2 group
on left hand side |
1 | 7739-7742 | These exist
both in ‘D’ and ‘L’ forms Most naturally occurring amino acids have
L-configuration L-Aminoacids are represented by writing the –NH2 group
on left hand side You have already read that proteins are the polymers of a-amino acids
and they are connected to each other by peptide bond or peptide
linkage |
1 | 7740-7743 | Most naturally occurring amino acids have
L-configuration L-Aminoacids are represented by writing the –NH2 group
on left hand side You have already read that proteins are the polymers of a-amino acids
and they are connected to each other by peptide bond or peptide
linkage Chemically, peptide linkage is an amide formed between
–COOH group and –NH2 group |
1 | 7741-7744 | L-Aminoacids are represented by writing the –NH2 group
on left hand side You have already read that proteins are the polymers of a-amino acids
and they are connected to each other by peptide bond or peptide
linkage Chemically, peptide linkage is an amide formed between
–COOH group and –NH2 group The reaction between two molecules of
similar or different amino acids, proceeds through
the combination of the amino group of one molecule
with the carboxyl group of the other |
1 | 7742-7745 | You have already read that proteins are the polymers of a-amino acids
and they are connected to each other by peptide bond or peptide
linkage Chemically, peptide linkage is an amide formed between
–COOH group and –NH2 group The reaction between two molecules of
similar or different amino acids, proceeds through
the combination of the amino group of one molecule
with the carboxyl group of the other This results in
the elimination of a water molecule and formation of
a peptide bond –CO–NH– |
1 | 7743-7746 | Chemically, peptide linkage is an amide formed between
–COOH group and –NH2 group The reaction between two molecules of
similar or different amino acids, proceeds through
the combination of the amino group of one molecule
with the carboxyl group of the other This results in
the elimination of a water molecule and formation of
a peptide bond –CO–NH– The product of the reaction
is called a dipeptide because it is made up of two
amino acids |
1 | 7744-7747 | The reaction between two molecules of
similar or different amino acids, proceeds through
the combination of the amino group of one molecule
with the carboxyl group of the other This results in
the elimination of a water molecule and formation of
a peptide bond –CO–NH– The product of the reaction
is called a dipeptide because it is made up of two
amino acids For example, when carboxyl group of
glycine combines with the amino group of alanine
we get a dipeptide, glycylalanine |
1 | 7745-7748 | This results in
the elimination of a water molecule and formation of
a peptide bond –CO–NH– The product of the reaction
is called a dipeptide because it is made up of two
amino acids For example, when carboxyl group of
glycine combines with the amino group of alanine
we get a dipeptide, glycylalanine If a third amino acid combines to a dipeptide, the product is called a
tripeptide |
1 | 7746-7749 | The product of the reaction
is called a dipeptide because it is made up of two
amino acids For example, when carboxyl group of
glycine combines with the amino group of alanine
we get a dipeptide, glycylalanine If a third amino acid combines to a dipeptide, the product is called a
tripeptide A tripeptide contains three amino acids linked by two peptide
linkages |
1 | 7747-7750 | For example, when carboxyl group of
glycine combines with the amino group of alanine
we get a dipeptide, glycylalanine If a third amino acid combines to a dipeptide, the product is called a
tripeptide A tripeptide contains three amino acids linked by two peptide
linkages Similarly when four, five or six amino acids are linked, the respective
products are known as tetrapeptide, pentapeptide or hexapeptide,
respectively |
1 | 7748-7751 | If a third amino acid combines to a dipeptide, the product is called a
tripeptide A tripeptide contains three amino acids linked by two peptide
linkages Similarly when four, five or six amino acids are linked, the respective
products are known as tetrapeptide, pentapeptide or hexapeptide,
respectively When the number of such amino acids is more than ten, then
the products are called polypeptides |
1 | 7749-7752 | A tripeptide contains three amino acids linked by two peptide
linkages Similarly when four, five or six amino acids are linked, the respective
products are known as tetrapeptide, pentapeptide or hexapeptide,
respectively When the number of such amino acids is more than ten, then
the products are called polypeptides A polypeptide with more than hundred
amino acid residues, having molecular mass higher than 10,000u is called
a protein |
1 | 7750-7753 | Similarly when four, five or six amino acids are linked, the respective
products are known as tetrapeptide, pentapeptide or hexapeptide,
respectively When the number of such amino acids is more than ten, then
the products are called polypeptides A polypeptide with more than hundred
amino acid residues, having molecular mass higher than 10,000u is called
a protein However, the distinction between a polypeptide and a protein is
not very sharp |
1 | 7751-7754 | When the number of such amino acids is more than ten, then
the products are called polypeptides A polypeptide with more than hundred
amino acid residues, having molecular mass higher than 10,000u is called
a protein However, the distinction between a polypeptide and a protein is
not very sharp Polypeptides with fewer amino acids are likely to be called
proteins if they ordinarily have a well defined conformation of a protein such
as insulin which contains 51 amino acids |
1 | 7752-7755 | A polypeptide with more than hundred
amino acid residues, having molecular mass higher than 10,000u is called
a protein However, the distinction between a polypeptide and a protein is
not very sharp Polypeptides with fewer amino acids are likely to be called
proteins if they ordinarily have a well defined conformation of a protein such
as insulin which contains 51 amino acids Proteins can be classified into two types on the basis of their
molecular shape |
1 | 7753-7756 | However, the distinction between a polypeptide and a protein is
not very sharp Polypeptides with fewer amino acids are likely to be called
proteins if they ordinarily have a well defined conformation of a protein such
as insulin which contains 51 amino acids Proteins can be classified into two types on the basis of their
molecular shape (a) Fibrous proteins
When the polypeptide chains run parallel and are held together by
hydrogen and disulphide bonds, then fibre– like structure is formed |
1 | 7754-7757 | Polypeptides with fewer amino acids are likely to be called
proteins if they ordinarily have a well defined conformation of a protein such
as insulin which contains 51 amino acids Proteins can be classified into two types on the basis of their
molecular shape (a) Fibrous proteins
When the polypeptide chains run parallel and are held together by
hydrogen and disulphide bonds, then fibre– like structure is formed Such
proteins are generally insoluble in water |
1 | 7755-7758 | Proteins can be classified into two types on the basis of their
molecular shape (a) Fibrous proteins
When the polypeptide chains run parallel and are held together by
hydrogen and disulphide bonds, then fibre– like structure is formed Such
proteins are generally insoluble in water Some common examples are
keratin (present in hair, wool, silk) and myosin (present in muscles), etc |
1 | 7756-7759 | (a) Fibrous proteins
When the polypeptide chains run parallel and are held together by
hydrogen and disulphide bonds, then fibre– like structure is formed Such
proteins are generally insoluble in water Some common examples are
keratin (present in hair, wool, silk) and myosin (present in muscles), etc 10 |
1 | 7757-7760 | Such
proteins are generally insoluble in water Some common examples are
keratin (present in hair, wool, silk) and myosin (present in muscles), etc 10 2 |
1 | 7758-7761 | Some common examples are
keratin (present in hair, wool, silk) and myosin (present in muscles), etc 10 2 3 Structure
of Proteins
Rationalised 2023-24
293
Biomolecules
Fig |
1 | 7759-7762 | 10 2 3 Structure
of Proteins
Rationalised 2023-24
293
Biomolecules
Fig 10 |
1 | 7760-7763 | 2 3 Structure
of Proteins
Rationalised 2023-24
293
Biomolecules
Fig 10 1: a-Helix
structure of proteins
Fig |
1 | 7761-7764 | 3 Structure
of Proteins
Rationalised 2023-24
293
Biomolecules
Fig 10 1: a-Helix
structure of proteins
Fig 10 |
1 | 7762-7765 | 10 1: a-Helix
structure of proteins
Fig 10 2: b-Pleated sheet structure of
proteins
(b) Globular proteins
This structure results when the chains of polypeptides coil around
to give a spherical shape |
1 | 7763-7766 | 1: a-Helix
structure of proteins
Fig 10 2: b-Pleated sheet structure of
proteins
(b) Globular proteins
This structure results when the chains of polypeptides coil around
to give a spherical shape These are usually soluble in water |
1 | 7764-7767 | 10 2: b-Pleated sheet structure of
proteins
(b) Globular proteins
This structure results when the chains of polypeptides coil around
to give a spherical shape These are usually soluble in water Insulin
and albumins are the common examples of globular proteins |
1 | 7765-7768 | 2: b-Pleated sheet structure of
proteins
(b) Globular proteins
This structure results when the chains of polypeptides coil around
to give a spherical shape These are usually soluble in water Insulin
and albumins are the common examples of globular proteins Structure and shape of proteins can be studied at four different
levels, i |
1 | 7766-7769 | These are usually soluble in water Insulin
and albumins are the common examples of globular proteins Structure and shape of proteins can be studied at four different
levels, i e |
1 | 7767-7770 | Insulin
and albumins are the common examples of globular proteins Structure and shape of proteins can be studied at four different
levels, i e , primary, secondary, tertiary and quaternary, each level
being more complex than the previous one |
1 | 7768-7771 | Structure and shape of proteins can be studied at four different
levels, i e , primary, secondary, tertiary and quaternary, each level
being more complex than the previous one (i) Primary structure of proteins: Proteins may have
one or more polypeptide chains |
1 | 7769-7772 | e , primary, secondary, tertiary and quaternary, each level
being more complex than the previous one (i) Primary structure of proteins: Proteins may have
one or more polypeptide chains Each polypeptide in a
protein has amino acids linked with each other in a
specific sequence and it is this sequence of amino acids
that is said to be the primary structure of that protein |
1 | 7770-7773 | , primary, secondary, tertiary and quaternary, each level
being more complex than the previous one (i) Primary structure of proteins: Proteins may have
one or more polypeptide chains Each polypeptide in a
protein has amino acids linked with each other in a
specific sequence and it is this sequence of amino acids
that is said to be the primary structure of that protein Any change in this primary structure i |
1 | 7771-7774 | (i) Primary structure of proteins: Proteins may have
one or more polypeptide chains Each polypeptide in a
protein has amino acids linked with each other in a
specific sequence and it is this sequence of amino acids
that is said to be the primary structure of that protein Any change in this primary structure i e |
1 | 7772-7775 | Each polypeptide in a
protein has amino acids linked with each other in a
specific sequence and it is this sequence of amino acids
that is said to be the primary structure of that protein Any change in this primary structure i e , the sequence
of amino acids creates a different protein |
1 | 7773-7776 | Any change in this primary structure i e , the sequence
of amino acids creates a different protein (ii) Secondary structure of proteins: The secondary
structure of protein refers to the shape in which a long
polypeptide chain can exist |
1 | 7774-7777 | e , the sequence
of amino acids creates a different protein (ii) Secondary structure of proteins: The secondary
structure of protein refers to the shape in which a long
polypeptide chain can exist They are found to exist in
two different types of structures viz |
1 | 7775-7778 | , the sequence
of amino acids creates a different protein (ii) Secondary structure of proteins: The secondary
structure of protein refers to the shape in which a long
polypeptide chain can exist They are found to exist in
two different types of structures viz a-helix and
b-pleated sheet structure |
1 | 7776-7779 | (ii) Secondary structure of proteins: The secondary
structure of protein refers to the shape in which a long
polypeptide chain can exist They are found to exist in
two different types of structures viz a-helix and
b-pleated sheet structure These structures arise due
to the regular folding of the backbone of the polypeptide
chain due to hydrogen bonding between
and
–NH– groups of the peptide bond |
1 | 7777-7780 | They are found to exist in
two different types of structures viz a-helix and
b-pleated sheet structure These structures arise due
to the regular folding of the backbone of the polypeptide
chain due to hydrogen bonding between
and
–NH– groups of the peptide bond a-Helix is one of the most common ways in which
a polypeptide chain forms all possible hydrogen bonds
by twisting into a right handed screw (helix) with the
–NH group of each amino acid residue hydrogen bonded to the
C O of an adjacent turn of the helix as shown in Fig |
1 | 7778-7781 | a-helix and
b-pleated sheet structure These structures arise due
to the regular folding of the backbone of the polypeptide
chain due to hydrogen bonding between
and
–NH– groups of the peptide bond a-Helix is one of the most common ways in which
a polypeptide chain forms all possible hydrogen bonds
by twisting into a right handed screw (helix) with the
–NH group of each amino acid residue hydrogen bonded to the
C O of an adjacent turn of the helix as shown in Fig 10 |
1 | 7779-7782 | These structures arise due
to the regular folding of the backbone of the polypeptide
chain due to hydrogen bonding between
and
–NH– groups of the peptide bond a-Helix is one of the most common ways in which
a polypeptide chain forms all possible hydrogen bonds
by twisting into a right handed screw (helix) with the
–NH group of each amino acid residue hydrogen bonded to the
C O of an adjacent turn of the helix as shown in Fig 10 1 |
1 | 7780-7783 | a-Helix is one of the most common ways in which
a polypeptide chain forms all possible hydrogen bonds
by twisting into a right handed screw (helix) with the
–NH group of each amino acid residue hydrogen bonded to the
C O of an adjacent turn of the helix as shown in Fig 10 1 In b-pleated sheet structure all peptide chains are
stretched out to nearly maximum extension and then
laid side by side which are held together by
intermolecular hydrogen bonds |
1 | 7781-7784 | 10 1 In b-pleated sheet structure all peptide chains are
stretched out to nearly maximum extension and then
laid side by side which are held together by
intermolecular hydrogen bonds The structure resembles
the pleated folds of drapery and therefore is known as
b-pleated sheet |
1 | 7782-7785 | 1 In b-pleated sheet structure all peptide chains are
stretched out to nearly maximum extension and then
laid side by side which are held together by
intermolecular hydrogen bonds The structure resembles
the pleated folds of drapery and therefore is known as
b-pleated sheet (iii) Tertiary structure of proteins: The tertiary
structure of proteins represents overall folding of the
polypeptide chains i |
1 | 7783-7786 | In b-pleated sheet structure all peptide chains are
stretched out to nearly maximum extension and then
laid side by side which are held together by
intermolecular hydrogen bonds The structure resembles
the pleated folds of drapery and therefore is known as
b-pleated sheet (iii) Tertiary structure of proteins: The tertiary
structure of proteins represents overall folding of the
polypeptide chains i e |
1 | 7784-7787 | The structure resembles
the pleated folds of drapery and therefore is known as
b-pleated sheet (iii) Tertiary structure of proteins: The tertiary
structure of proteins represents overall folding of the
polypeptide chains i e , further folding of the secondary
structure |
1 | 7785-7788 | (iii) Tertiary structure of proteins: 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 |
1 | 7786-7789 | e , further folding of the secondary
structure It gives rise to two major molecular shapes
viz fibrous and globular |
1 | 7787-7790 | , further folding of the secondary
structure It gives rise to two major molecular shapes
viz fibrous and globular The main forces which
stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals
and electrostatic forces of attraction |
1 | 7788-7791 | It gives rise to two major molecular shapes
viz fibrous and globular The main forces which
stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals
and electrostatic forces of attraction (iv) Quaternary structure of proteins: Some of the
proteins are composed of two or more polypeptide
chains referred to as sub-units |
1 | 7789-7792 | fibrous and globular The main forces which
stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals
and electrostatic forces of attraction (iv) Quaternary structure of proteins: Some of the
proteins are composed of two or more polypeptide
chains referred to as sub-units The spatial
arrangement of these subunits with respect to each
other is known as quaternary structure |
1 | 7790-7793 | The main forces which
stabilise the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals
and electrostatic forces of attraction (iv) Quaternary structure of proteins: Some of the
proteins are composed of two or more polypeptide
chains referred to as sub-units The spatial
arrangement of these subunits with respect to each
other is known as quaternary structure Rationalised 2023-24
294
Chemistry
Fig |
1 | 7791-7794 | (iv) Quaternary structure of proteins: Some of the
proteins are composed of two or more polypeptide
chains referred to as sub-units The spatial
arrangement of these subunits with respect to each
other is known as quaternary structure Rationalised 2023-24
294
Chemistry
Fig 10 |
1 | 7792-7795 | The spatial
arrangement of these subunits with respect to each
other is known as quaternary structure Rationalised 2023-24
294
Chemistry
Fig 10 3: Diagrammatic representation of protein structure (two sub-units
of two types in quaternary structure)
A diagrammatic representation of all these four structures is
given in Figure 10 |
1 | 7793-7796 | Rationalised 2023-24
294
Chemistry
Fig 10 3: Diagrammatic representation of protein structure (two sub-units
of two types in quaternary structure)
A diagrammatic representation of all these four structures is
given in Figure 10 3 where each coloured ball represents an
amino acid |
1 | 7794-7797 | 10 3: Diagrammatic representation of protein structure (two sub-units
of two types in quaternary structure)
A diagrammatic representation of all these four structures is
given in Figure 10 3 where each coloured ball represents an
amino acid Fig |
1 | 7795-7798 | 3: Diagrammatic representation of protein structure (two sub-units
of two types in quaternary structure)
A diagrammatic representation of all these four structures is
given in Figure 10 3 where each coloured ball represents an
amino acid Fig 10 |
1 | 7796-7799 | 3 where each coloured ball represents an
amino acid Fig 10 4: Primary,
secondary, tertiary
and quaternary
structures of
haemoglobin
Protein found in a biological system with a unique three-dimensional
structure and biological activity is called a native protein |
1 | 7797-7800 | Fig 10 4: Primary,
secondary, tertiary
and quaternary
structures of
haemoglobin
Protein found in a biological system with a unique three-dimensional
structure and biological activity is called a native protein 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 |
1 | 7798-7801 | 10 4: Primary,
secondary, tertiary
and quaternary
structures of
haemoglobin
Protein found in a biological system with a unique three-dimensional
structure and biological activity is called a native protein 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 |
1 | 7799-7802 | 4: Primary,
secondary, tertiary
and quaternary
structures of
haemoglobin
Protein found in a biological system with a unique three-dimensional
structure and biological activity is called a native protein 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
10 |
1 | 7800-7803 | 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
10 2 |
1 | 7801-7804 | Due to this, globules unfold and helix get uncoiled
and protein loses its biological activity This is called denaturation of
10 2 4
Denaturation of
Proteins
Rationalised 2023-24
295
Biomolecules
protein |
1 | 7802-7805 | This is called denaturation of
10 2 4
Denaturation of
Proteins
Rationalised 2023-24
295
Biomolecules
protein During denaturation secondary and tertiary structures are
destroyed but primary structure remains intact |
1 | 7803-7806 | 2 4
Denaturation of
Proteins
Rationalised 2023-24
295
Biomolecules
protein During denaturation secondary and tertiary structures are
destroyed but primary structure remains intact The coagulation of
egg white on boiling is a common example of denaturation |
1 | 7804-7807 | 4
Denaturation of
Proteins
Rationalised 2023-24
295
Biomolecules
protein During denaturation secondary and tertiary structures are
destroyed but primary structure remains intact The coagulation of
egg white on boiling is a common example of denaturation Another
example is curdling of milk which is caused due to the formation of
lactic acid by the bacteria present in milk |
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