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Tertiary Protein Structure

Tertiary Protein Structure


Refers to three-dimensional structure of a single protein molecule. Result from the interactions between amino acid side chain that are widely separated from each other with a peptide chain.

Interaction Responsible for Tertiary Structure

Disulfide bonds Hydrophobic interactions Hydrogen bonds Ionic Bond

Covalent Disulfide bonds


usually formed from theoxidationofsulfhydryl (-SH) groups 2 RSH RS-SR + 2 H++ 2 e-

Covalent Disulfide bonds

Hydrogen bond
Attractive interaction of ahydrogenatom with anelectronegativeatom, such as nitrogen,oxygenorfluorine, that comes from another molecule orchemical group

Hydrogen bond

Ionic Bond
a type ofchemical bondformed through anelectrostaticattraction between two oppositely chargedions. Also called salt bridge, always involve the interaction between acidic side chain and a basic side chain. COOH = COO- and NH2 = NH3+

Ionic Bond

Hydrophobic interactions
Result when two non polar side chains are close to each other. In aqueous solution, many proteins have their polar R groups outward, toward the aqueous solvent and their non polar R groups inward. The non polar R groups then interact with each other.

Protein Hydrolysis
the breakdown of protein into smaller peptides and free amino acid.

Protein Denaturation
Involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a

Protein Denaturation
Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and nonpolar hydrophobic interactions. which may be disrupted. Therefore, a variety of reagents and conditions can cause denaturation.

Protein Denaturation Factors


Heat Alcohol Disrupts Hydrogen Bonding Acids and Bases Disrupt Salt Bridges Reducing Agents Disrupt Disulfide Bonds

Heat
Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted. The proteins in eggs denature and coagulate during cooking. Other foods are cooked to denature the proteins to make it easier for enzymes to digest them. Medical supplies and instruments are sterilized by heating to denature proteins in bacteria and thus destroy

Alcohol Disrupts Hydrogen Bonding


Hydrogen bonding occurs between amide groups in the secondary protein structure. Hydrogen bonding between "side chains" occurs in t ertiary protein structurein a variety of amino acid combinations. All of these are disrupted by the addition of another alcohol.

Alcohol Disrupts Hydrogen Bonding


A 70% alcohol solution is used as a disinfectant on the skin. This concentration of alcohol is able to penetrate the bacterial cell wall and denature the proteins and enzymes inside of the cell. A 95% alcohol solution merely coagulates the protein on the outside of the cell wall and prevents any alcohol from entering the cell. Alcohol denatures proteins by disrupting the side chain intramolecular hydrogen bonding. New hydrogen bonds are formed instead between the new alcohol

What is the difference between the alpha-helix and the beta-sheet protein conformations?
Alpha-helix and beta-sheet conformationsare thetwo main types of secondary structure of a protein molecule. According to the primary protein structure its secondary structure can be of one type or the other. In the alpha-helix structure the polypeptide curls longitudinally by the action of hydrogen bonds forming a spiral, or helix. In the beta-sheet conformation the protein is more distended and the hydrogen bonds form a zig-zag-shaped protein structure called B-strand. Many assembled beta-strands make a beta-sheet.

What is protein denaturation? Is there any change in the primary structure when a protein is denatured? Secondary, tertiary and quaternary structures of proteins are spatial structures. Denaturation is modification in any of these spatial structures that makes the protein deficient or biologically inactive. After denaturation the primary protein structure is not affected.

In an ionic bond, the atoms are bound together by the attraction between oppositely-charged ions. For example, sodium and chloride form an ionic bond, to make NaCl, or table salt. In a covalent bond, the atoms are bound by shared electrons. If the electron is shared equally between the atoms forming a covalent bond, then the bond is said to be nonpolar. Usually, an electron is more attracted to one atom than to another, forming a polar covalent bond. For example, the atoms in water, H2O, are held

What Is the Difference Between an Ionic and Covalent Chemical Bond?