Protein, it's an important part of life and nutrition;we can get it from food. it is the substance that composes a large portion of your body’s structure. Proteins are made up of amino acids arranged in different
combinations. Next to water, protein is the most abundant substance in the human body. It is part of all body cells and is a vital building block in the growth, maintenance and repair of the body
The monomer of the protein is amino acids.
Basically, protein is form by 5 elements:
-Hydrogen
-Nitrogen
-Carbon
-Carboxyl
-R group (other elements)
R group is a symbol for other elements. Each element that connect to protein, will form different kind of protein. So, different element means different type of protein. There are 20 types of protein. The bond that form by the R group, will stronger than the hydrogen bond. hydrogen bond is a relatively weak bond formed by the attraction between a group wit a small positive charge on a hydrogen atom and other group carrying a small negative charge. This are the types of protein that cause by the different element ( R group)
There are 2 kind of reaction that will happened in this kind of situation (protein):
-Hydrolysis
-Condensation
Hydrolysis is a process or reaction that will happened to break down the dipeptide. it will give the H2O to the dipeptide (2 amino acids that combined together). So, the dipeptide become 2 single amino acids.
Condensation is a process to built the dipeptide by take the H2O from 2 amino acids, and combined the 2 amino acids, become dipeptide, form "peptide bond"(bond that link 2 amino acid together after take the H2O.
Peptide bond, is a bond that form by 2 amino acids, after condensation process.
Dipeptide bond, is a bond that form by 2 dipeptide.
Polypeptide bond, is a bond that form by 2 polypeptide.
There 4 types of protein structure as well:
-Primary
-Secondary
-Tertiary
-Quartenary
Primary structure is the simplest one, and Quartenary structure is the most complicated one.
Primary Structure:
(biochemistry) A structure of a
biological molecule in which there is a precise
sequence or order
of monomeric units. It serves as the covalent backbone of biologicalmolecules (such
as DNA and proteins).
Example: Hemoglobin
A structure of a biological molecule characterized by the local folding within the biopolymer as a result of
Example: Myoglobin
A
structural level wherein several proteins (or polypeptide subunits) interact through non-covalent
bonds to form one functional protein complex.
Example: Complex Hemoglobin
Tertiary Structure:
A structure of a biological molecule (such as proteins and nucleic acids) which is in its three dimensional shape, as defined by the atomic coordinates.
Example: Human Insulin
To make it more detail, it's better for you to know the definition of:
ionic bond, hydrogen bond, disulfide bonds, hydrophobic interactions :
ionic bond, hydrogen bond, disulfide bonds, hydrophobic interactions :
References:
https://www.health.arizona.edu/health_topics/nutrition/sports/protein.pdf
http://www.elmhurst.edu/~chm/vchembook/161Ahydrogenbond.html
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/P/PrimaryStructure.html
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/S/SecondaryStructure.html
