Denaturation of Proteins

Question 1

the building blocks of protein molecules are the

Answer 1

alpha-amino acids

Question 2

Structures of Proteins

Answer 2

• Primary Protein Structure
• Secondary Protein Structure
• Tertiary Protein Structure

Question 3

is the actual sequence of its amino acid

Answer 3

Primary Protein Structure

Question 4

is determined by the order of the deoxyribonucleotide bases in genes

Answer 4

Primary Protein Structure

Question 5

is due to hydrogen bonds that form between the oxygen atom of one amino acid and the nitrogen atom of another

Answer 5

secondary protein structure

Question 6

this gives the proein or polypeptide the two-dimensional form of an

Answer 6

alpha-helix or a beta-pleated sheet

Question 7

two possible types of seccondary structure

Answer 7

alpha-helix and beta-pleated sheet

Question 8

cause the polypeptide to twist into a helix

Answer 8

alpha-helix

Question 9

the hydrogen bonding enables the polypetide to fold backa dn forth upon itself like a pleated sheet

Answer 9

beta-pleated sheet

Question 10

is determined by a variety of chemical interactions. these include hydrophobic interactions, ionic bonding, hydrigen bonding, and disulfide linkages

Answer 10

tertiary protein stucture

Question 11

tertiary protein stucture is determined by a variety of chemical interactions. these include:

Answer 11

hydrophobic interactions, ionic bonding, hydrigen bonding, and disulfide linkages

Question 12

These amino acids are joined together by bonds between the carboxyl group of one amino acid and the amino group of another, with splitting off of wate

Answer 12

alpha- amino acids.

Question 13

is a molecule containing an amino group and a carboxylic acid group that are separated by one carbon, called the α-carbon

Answer 13

alpha-amino acid

Question 14

An alpha-amino acid is a molecule containing an amino group and a carboxylic acid group that are separated by one carbon

Answer 14

α-carbon

Question 15

Each amino acid is linked to the next amino acid through _____________________ created during the protein biosynthesis process.

Answer 15

peptide bonds

Question 16

Each amino acid is linked to the next amino acid
through peptide bonds created during the

Answer 16

protein biosynthesis process.

Question 17

The number of polypeptide chains together form

Answer 17

proteins

Question 18

Any change in the sequence _____________________________

Answer 18

changes the entire protein

Question 19

All documented genetic disorders, such as cystic fibrosis, sickle cell anemia, albinism, etc., are caused by _____________ resulting in ______________________________________, which in turn lead to alterations in the secondary , tertiary and probably quarterly structure.

Answer 19

mutations; alterations in the primary protein structures

Question 20

is due to hydrogen bonds that form between the oxygen
atom of one amino acid and the nitrogen atom
of another

Answer 20

secondary structure of the protein

Question 21

The secondary structure of the protein is due to hydrogen bonds that form between the _____________________of one amino acid and the _____________ of another.

Answer 21

oxygen atom; nitrogen atom

Question 22

The secondary structure of the protein is due to
hydrogen bonds that form between the oxygen
atom of one amino acid and the nitrogen atom
of another. This gives the protein or polypeptide
the two-dimensional form of an

Answer 22

alpha-helix or a beta-pleated sheet

Question 23

The proteins _____________ exist in just simple
chains of polypeptides

Answer 23

do not

Question 24

is one of the most common ways in
which a polypeptide chain forms all possible
hydrogen bonds by twisting into a right-handed
screw with the -NH group of each amino acid
residue hydrogen-bonded to the -CO of the
adjacent turn of the helix. The polypeptide
chains twisted into a right-handed screw.

Answer 24

α – Helix

Question 25

In this arrangement, the polypeptide chains are
stretched out beside one another and then
bonded by

Answer 25

intermolecular H-bonds.

Question 26

In this arrangement, the polypeptide chains are
stretched out beside one another and then
bonded by intermolecular H-bonds. The
structure resembles the pleated folds of drapery
and therefore is known as

Answer 26

β – pleated sheet

Question 27

Many proteins contain both ________________________________, though some contain jus ________________________

Answer 27

α helices and β pleated sheets; one type of
secondary structure

Question 28

is determined by a variety of chemical interactions. These
include hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages.

Answer 28

tertiary structure of proteins

Question 29

The tertiary structure of proteins is determined
by a variety of chemical interactions. These
include

Answer 29

hydrophobic interactions, ionic bonding,
hydrogen bonding, and disulfide linkages

Question 30

The overall three-dimensional arrangement of
its polypeptide chain in space, once all the
secondary structure elements have folded
together among each other will create the
complex

Answer 30

three-dimensional tertiary structure of a
protein

Question 31

is due to several polypeptides joining together, as in the
case of antibody molecules.

Answer 31

quaternary structure of a protein

Question 32

It exists in proteins consisting of two or more identical or different polypeptide chains (subunits).

Answer 32

quaternary structure of a protein

Question 33

is the association of several protein chains or subunits
into a closely packed arrangement

Answer 33

quaternary structure of a protein

Question 34

sequence of a chain of amino acids

Answer 34

primary protein structure

Question 35

hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern

Answer 35

secondary protein structure

Question 36

three-dimensional folding pattern of a protein due to side chain reactions

Answer 36

tertiary protein structure

Question 37

protein consisting of more than one amino acid chain

Answer 37

quaternary protein structure

Question 38

A protein has a _____________________ regardless of
the amount of substance present in the solid
phase.

Answer 38

constant solubility

Question 39

A protein has a constant solubility regardless of
the amount of substance present in the solid
phase. This property is a sensitive test for the
presence of

Answer 39

protein impurity

Question 40

Proteins can be hydrolyzed by using

Answer 40

acids,
alkalies, and enzymes

Question 41

Proteins can be precipitated by

Answer 41

acids, salts of
heavy metals, alcohols, and neutral salts.

Question 42

When a protein loses its higher-order structure, but not its primary sequence, it is said to be

Answer 42

denatured

Question 43

Denatured proteins are usually

Answer 43

non-functional

Question 44

is one of the
phenomenons that results in the disturbance of
stability and structure of the protein

Answer 44

Denaturation of proteins

Question 45

is the change in the
chemical, physical, and biological
properties of a protein from those of the
native state, characterized by an unfolding
of the molecule from its previous
configuration

Answer 45

denaturation

Question 46

Physical Denaturing Agents

Answer 46

• Heat
• Light
• Surface action
• High pressure
• Mechanical agitation

Question 47

Chemical Denaturing Agents

Answer 47

• Organic solvents (alcohol, acetone,
  ether)
• Acids and Alkalies
• Salts and heavy metals
• Enzymes
• Detergents
• Urea and guanidine