Properties of proteins

Physical Properties of Proteins

Proteins are colorless and tasteless.

They are homogeneous and crystalline.
Proteins vary in shape, they may be simple crystalloid structure to long
fibrilar structures.
Protein structures are of two distinct patterns - Globular proteins and fibrilar
proteins.
Globular proteins are spherical in shape and occur in plants. Fibrilar proteins
are thread-like, they occur generally in animals.
In general proteins have large molecular weights ranging between 5 X 10 3
and 1 X 106.
Due to the huge size, proteins exhibit many colloidal properties.
The diffusion rates of proteins is extremely slow.
Proteins exhibit Tyndall effect.
Proteins tend to change their properties like denaturation. Many a times the
process of denaturation is followed by coagulation.
Denaturation may be a result of either physical or chemical agents. The
physical agents include, shaking, freezing, heating etc. Chemical agents are
like X-rays, radioactive and ultrasonic radiations.
Proteins like the amino acids exhibit amphoteric property i.e., they can act as
acids and alkalies.
As the proteins are amphoteric in nature, they can form salts with both
cations and anions based on the net charge.
The solubility of proteins depends upon the pH. Lowest solubility is seen at
isoelectric point, the solubility increases with increase in acidity or alkalinity.
All the proteins show the plane of polarized light to the left, i.e.,
laevorotatory.
Chemical Properties of Proteins
Proteins when hydrolyzed by acidic agents, like conc.HCl yield amino acids in
the form of their hydrochlorides.
Proteins when are hydrolyzed with alkaline agents leads to hydrolysis of
certain amino acids like arginie, cysteine, serine, etc., also the optical activity
of the amino acids is lost.
Proteins with reaction with alcohols gives its corresponding esters. This
process is known as esterification.
Amino acids reacts with amines to form amides.
When free amino acids or proteins are said to react with mineral acids like
HCl, the acid salts are formed.
When amino acids in alkaline medium reacts with many acid chlorides,
acylation reaction takes place.
Sanger's reaction - Proteins react with FDNB reagent to produce yellow
colored derivative, DNB amino acid.
Xanthoproteic test - On boiling proteins with conc. HNO 3, yellow color
develops due to presence of benzene ring.
Folin's test - This is a specific test for tyrosine amino acid, where blue color
develops with phosphomolybdotungstic acid in alkaline solution due to
presence of phenol group.
Denaturation
A protein is denatured when its specific three-dimensional conformation is
changed by breaking some bonds without breaking its primary structure. It
may be, for example, the disruption of helix areas. The denaturation may be
reversible or irreversible. It causes a total or partial loss of biological activity.
This is an important property of protein.
Denaturing agents:
Physical agents: Heat, radiation, pH
Chemical agents: Urea solution which forms new hydrogen bonds in the
protein,
organic solvents, detergents
Denaturants
Acids
Acetic acid
Acidic protein denaturants
Trichloroacetic acid 12% in
include:
water

 Sulfosalicylic acid
Bases
Bases work similarly to acids in
denaturation. They include:
Sodium bicarbonate
Solvents
Most organic solvents are denaturing,
Ethanol
Alcohol
Cross-linking reagents
Cross-linking agents for proteins
include
Formaldehyde

Glutaraldehyde
Chaotropic agents
Chaotropic agents include
Urea 6 8 mol/l
Guanidinium chloride 6 mol/l
Lithium perchlorate 4.5 mol/l
Disulfide bond reducers
Agents that break disulfide bonds by
reduction include:
2-Mercaptoethanol
Dithiothreitol
TCEP (tris(2carboxyethyl)phosphine)

Structure of Proteins
Primary Structure of Protein
Primary structure of protein is the linear sequence of amino acids that make
up the polypeptide chain.
his sequence is given by the sequence of nucleotide bases of the DNA in the
genetic code.
The amino acid sequence determines the positioning of the different R groups
relative to each other.
The positioning determines the way the protein folds and the final structure
of the molecule.
Secondary Structure of Protein
The linear, unfolded structure of polypeptide chain assumes helical shape to
produce the secondary structure.
The secondary structure refers to the regular folding pattern of twists and
kinks of the polypeptide chain.
The regular pattern is due to the hydrogen bond formation between atoms of
the amino acid backbone of the polypeptide chain.
The most common types of the secondary structure are the alpha helix and
the pleated sheet.
Tertiary Structure of Protein
Tertiary structure of proteins is the three dimensional structure formed by the
bending and twisting of the polypeptide chain.
The linear sequence of polypeptide chain is folded into compact globular
structure.
The folding of the polypeptide chain is stabilized by weak, noncovalent
interactions.
These interactions are hydrogen bonds and electrostatic interactions.

Hydrogen bonds are formed when hydrogen atom is shared with two other
atoms.
Electrostatic interactions between charged amino acid chains.
Electrostatic interactions are between positive and negative ions of the
macromolecules.
Hydrophobic interactions, disulphide linkages and covalent bonds also
contribute to tertiary structure.
Quaternary Structure of Protein
Some proteins contain more than one polypeptide chains, this association of
polypeptide chains refers to the quaternary structure.
Each polypeptide chain is called a subunit.
The subunits can be same or different ones.
Example: Haemoglobin the oxygen carrying component of blood is made up of two
polypeptide chains, one with 141 amino acids and the other is a different type of
146 amino acids.
Physical Properties of Proteins
Solubility in Water
The relationship of proteins with water is complex. The secondary structure of
proteins depends largely on the interaction of peptide bonds with water
through hydrogen bonds.
Hydrogen bonds are also formed between protein (alpha and beta structures)
and water. The protein-rich static ball are more soluble than the helical
structures.
At the tertiary structure, water causes the orientation of the chains and
hydrophilic radicals to the outside of the molecule, while the hydrophobic
chains and radicals tend to react with each other within the molecule (cf.
hydrophobic effect).
The solubility of proteins in an aqueous solution containing salts depends on
two opposing effects on the one hand related to electrostatic interactions
("salting in") and other hydrophobic interactions (salting out)