The a-helix of proteins is

Both α-helix and β-pleated sheet conformation of proteins were proposed by

Denaturation of proteins results in

In a protein molecule the disulphide bond
is not broken by

The apolipoprotein which acts as ligand
for LDL receptor is

The apolipoprotein which from the
integral component of VLDL is

Globular proteins have completely folded,
coiled polypeptide chain and the axial
ratio (ratio of length to breadth) is

The apolipoprotein which forms the
integral component of chylomicron is

Ceruloplasmin is

The apolipoprotein which acts as activator
of LCAT is

The lipoprotein with the fastest electrophoretic mobility and the lowest triglyceride content is

Fibrous proteins have axial ratio

Distance traveled per turn of α−helix in
nm is

In proteins the α-helix and β-pleated sheet
are examples of

Serum LDL has been found to be increased
in

the number of helices present in a
collagen molecule is

Tertiary structure of a protein describes

Each turn of α-helix contains the amino
acid residues (number):

At the lowest energy level α-helix of
polypeptide chain is stabilised

Along the α-helix each amino acid residue
advances in nm by

The lipoprotein associated with activation
of LCAT is

The technique for purification of proteins
that can be made specific for a given
protein is

The hydrogen bonds between peptide
linkages of a protein molecules are interfered by

The primary structure of fibroin, the
principal protein of silk worm fibres
consists almost entirely of

The apolipoprotein which acts as activator
of extrahepatic lipoprotein is