Covers protein composition: amino acids, peptide bonds and polypeptide chains, and the classes of amino acids by side-chain polarity and charge. It then goes through covalent and noncovalent bonds in protein structure, a list of protein functions, and primary structure, using haemoglobin A and S and insulin as examples. It ends with four multiple-choice questions and their answers.
Topic 2 of 70 in the MU Sofia syllabus for Biochemistry (Medicine, Year 2). The free AceMed note covers it in 13 sections, about 1,068 words (8 min of reading), with 14 flashcards.
In this note
Proteins: Significance and Composition
Covalent Bonds and Noncovalent Interactions:
Functions in brief:
Non Polar amino acids
Polar amino acids
Electrically charged (acidic):
Electrically charged (basic):
Characteristic features of the polypeptide chains:
Primary Structure
Differences in the primary structure of hemoglobin A and S:
Insulin and diabetes mellitus. Primary structure of insulin in different species.:
MCQs ☺
Answers
Proteins: Significance and Composition
Proteins are heterobiopolymers formed by two or more different polymers (amino acids).
There are 20 types of amino acids in proteins, each with different chemical properties due to their structural differences.
They are made up of amino acids, which are organic compounds containing an amino group (-NH2), a carboxyl group (-COOH), and a variable side chain (R group).
Amino acids are linked together by covalent peptide bonds to form polypeptides.
Proteins have various functions, including structural support, transport, defense, regulation, catalysis, movement, and storage.
Amino acids are classified into nonpolar, polar, acidic, and basic categories based on the chemical structure and polarity of their side chains.
Covalent Bonds and Noncovalent Interactions:
Covalent bonds, such as peptide bonds, are the strongest type of chemical bonds in proteins and hold amino acids together.
These bonds are formed between the carboxyl group of one amino acid and the amino group of another, resulting in a covalent bond between the two amino acids.
In secondary protein structures: There are hydrogen bonds presents, peptide bonds and disulfide bonds
In tertiary structures: There are hydrophobic bonds, hydrogen bonds, ionic bonds, vaan der waals forces, disulfide bonds
The same type of bonds can be found in quaternary structures
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