Secondary protein structures occur when protein chains coil or fold
When protein chains called polypeptides join together, the tertiary structure forms because R groups interact with each other
In the watery environment of a cell, proteins become globular in their quaternary structure
Slide 60
Protein Structures or CONFORMATIONS
Hydrogen bond
Pleated sheet
Amino acid
(a) Primary structure
Hydrogen bond
Alpha helix
(b) Secondary structure
Polypeptide
(single subunit)
(c) Tertiary structure
(d) Quaternary structure
Slide 61
Changes in temperature & pH can denature (unfold) a protein so it no longer works
Cooking denatures protein in eggs
Milk protein separates into curds & whey when it denatures
Slide 62
Changing Amino Acid Sequence
Substitution of one amino acid for another in hemoglobin causes sickle-cell disease
(a) Normal red blood cell
Normal hemoglobin
1
2
3
4
5
6
7. . . 146
(b) Sickled red blood cell
Sickle-cell hemoglobin
2
3
1
4
5
6
7. . . 146
Slide 63
Blood sugar level is controlled by a protein called insulin
Insulin causes the liver to uptake and store excess sugar as Glycogen
The cell membrane also contains proteins
Receptor proteins help cells recognize other cells
Slide 64
INSULIN
Cell membrane with proteins & phospholipids
Slide 65
Store hereditary information
Contain information for making all the body’s proteins
Two types exist --- DNA & RNA
Slide 66
Slide 67
Nitrogenous base
(A,G,C, or T)
Phosphate
group
Thymine (T)
Sugar
(deoxyribose)
Phosphate
Base
Sugar
Nucleic acids are polymers of nucleotides
Nucleotide
Slide 68
Nucleotide – Nucleic acid monomer
Slide 69
Nucleic Acids
Slide 70