Covalently linked polymers of amino acids
Proteins
Bonds between amino acids in protein
peptide bond
_____ is removed - peptide bond
Water
Protein
● Different amino acids compose a specific protein in a linear manner.
Primary structure
● It is a folded primary structure
● The peptide chains are folded regularly and that is the time where there is a formation of ______ (2)
Secondary structure
α-helix and β-pleated sheets
Secondary structure
● Commonly formed structures stabilized by hydrogen bonds between the _____ (2)
amino acids within the protein
A secondary structure folded into a three-dimensional form.
Tertiary structure
A result from the interaction of side chains, which are stabilized through the hydrophobic effect, ionic attraction, hydrogen bonds, and disulfide bonds.
● Definitely a polypeptide
● Refers to the overall shape, or conformation, of the protein molecule.
Tertiary structure
● A combined tertiary structures or combined polypeptides
QUATERNARY STRUCTURE
CLASSIFICATION OF PROTEINS (COMPOSITION)
Simple
Conjugated
• SIMPLE
CONJUGATED
■ Lipids ()
■ CHO ()
■ Porphyrins ()
■ Metals ()
lipoprotein
glycoprotein
hemoglobin
ceruloplasmin
CLASSIFICATION OF PROTEINS (FUNCTION)
THE BOSS EI
Transport proteins
Hormones
Enzymes
Blood coagulation
Osmotic force
Storage proteins
Structural proteins
Energy source
Immunoglobulins
FIVE FRACTIONS OF PLASMA PROTEINS
● Albumin
● α1-Globulins
● α2-Globulins
● β-Globulins
● γ-Globulins
● α1-Globulins
○ α1-fetoprotein
○ α-antitrypsin
○ HDL
● α2-Globulins
HaCeMa
○ Haptoglobin
○ Ceruloplasmin
○ α2-macroglobulin
β-Globulins
CT
○ Transferrin
○ C-reactive protein
γ-Globulins
○ Immunoglobulins
PREALBUMIN
• Also known as
transthyretin
• Also known as transthyretin
PREALBUMIN
• Migrates ahead of albumin
• Transport protein of thyroid hormones
• Binds with retinol-binding protein to form a complex that transports retinol (vitamin A)
• Rich in tryptophan
PREALBUMIN
• Present in highest concentration
ALBUMIN