HomeProteinThe Secondary Structure Of A Protein Results From
February 1, 2018
The Secondary Structure Of A Protein Results From
The Secondary Structure Of A Protein Results From – The term structure when used in relation to proteins, takes on a much more complex meaning than it does for small molecules. Proteins are macromolecules and have four different levels of structure – primary, secondary, tertiary and quaternary. The primary structure of a protein is its linear sequence of specific amino acids. A single amino acid is shown to the right. The “side chain” is the portion that is different in each of the 20 different amino acids.
The Secondary Structure Of A Protein Results From – Secondary structure, refers to local folded structures that form within a polypeptide due to interactions between atoms of the backbone.
Hydrogen bonds belong to the class of intermolecular forces that arise as a result of a moleculeís dipolar characteristic. Hydrogen bonds exist between the hydrogen atom in a polar molecule such as (NH) and an unshared pair of electrons in a nearby (highly electronegative atom) such as Nitrogen, Oxygen or Fluorine. The polarity of a covalent bond is the result of the difference in electronegativity between the atoms that are bonded together. Electronegativity is defined as the ability of an atom (in a molecule) to attract shared electrons to itself.
Hydrogen bonding create Secondary Structure Of A Protein
Hydrogen bonds provide most of the directional interactions that underpin protein folding, protein structure and molecular recognition. The core of most protein structures is composed of secondary structures such as α helix and β sheet. This satisfies the hydrogen-bonding potential between main chain carbonyl oxygen and amide nitrogen buried in the hydrophobic core of the protein. Hydrogen bonding between a protein and its ligands (protein, nucleic acid, substrate, effector or inhibitor) provides a directionality and specificity of interaction that is a fundamental aspect of molecular recognition.
The energetics and kinetics of hydrogen bonding therefore need to be optimal to allow the rapid sampling and kinetics of folding, conferring stability to the protein structure and providing the specificity required for selective macromolecular interactions.