Biochemistry · MU Plovdiv

1. Proteins – functions and structure. Amino acids – types and classification. Biologically important oligopeptides and polypeptides. Molecular forms of proteins (hetero-, iso- and alloproteins). Levels of protein structures. Examples of proteins with quaternary structure – lactate dehydrogenases and hemoglobin. Denaturation of the proteins.

Inside: 24 sections · 9 labelled pictures · 36 flashcards · 13 min

Topic 1 of 63 in the MU Plovdiv syllabus for Biochemistry (Dental Medicine, Year 2). The free AceMed note covers it in 24 sections, about 1,786 words (13 min of reading), with 36 flashcards.

In this note

  1. Proteins: Significance and Composition
  2. Covalent Bonds and Noncovalent Interactions:
  3. Functions in brief:
  4. Non Polar amino acids
  5. Polar amino acids
  6. Electrically charged (acidic):
  7. Electrically charged (basic):
  8. Characteristic features of the polypeptide chains:
  9. Primary Structure
  10. Differences in the primary structure of hemoglobin A and S:
  11. Insulin and diabetes mellitus. Primary structure of insulin in different species.:
  12. MCQs ☺
  13. Answers
  14. SECONDARY, TERTIARY, AND QUATERNARY STRUCTURE OF PROTEINS:
  15. GLOBULAR AND FIBROUS PROTEINS:
  16. STRUCTURE AND FUNCTION OF HEMOGLOBIN:
  17. GLYCATED HEMOGLOBIN
  18. DEFECTS IN COLLAGEN BIOSYNTHESIS - SCURVY:
  19. DENATURATION AND RENATURATION:
  20. SICKLE CELL ANEMIA:
  21. PRION DISEASE
  22. RELATIONSHIP BETWEEN PROTEIN STRUCTURE AND FUNCTION:
  23. MCQ
  24. 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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