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Learning goals:
Structure and naming of amino acids Structure and properties of peptides Ionization behavior of amino acids and peptides Methods to characterize peptides and proteins
Transport
hemoglobin (transports O2 in the blood) lactose permease (transports lactose across the cell membrane)
Structure
collagen (connective tissue) keratin (hair, nails, feathers, horns)
Motion
myosin (muscle tissue) actin (muscle tissue, cell motility)
These amino acids side chains can form hydrogen bonds. Cysteine can form disulfide bonds.
Buffer Regions
than two pH units apart Why is the side chain pKa so much higher?
Formation of Peptides
Peptides are small condensation products of amino acids They are small compared to proteins (Mw < 10 kDa)
For longer peptides (like proteins) the oneletter code can be used
SGYAL
Neuropeptides
substance P (pain mediator)
Antibiotics
polymyxin B (for Gram bacteria) bacitracin (for Gram + bacteria)
Proteins are:
Polypeptides (covalently linked -amino acids) + possibly:
cofactors
functional non-amino acid component metal ions or organic molecules organic cofactors NAD+ in lactate dehydrogenase
coenzymes
prosthetic groups
other modifications
Column Chromatography
Separation by Charge
Separation by Size
Separation by Affinity
Protein Sequencing
It is essential to further biochemical analysis that we know the sequence of the protein we are studying Actual sequence generally determined from DNA sequence Edman Degradation (Classical method)
Successive rounds of N-terminal modification, cleavage, and identification Can be used to identify protein with known sequence
Edmans Degradation
Chapter 3: Summary
In this chapter, we learned about: The many biological functions of peptides and proteins The structures and names of amino acids found in proteins The ionization properties of amino acids and peptides The methods for separation and analysis of proteins