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2.4 Proteins

QuestionAnswer
proteome entire set of proteins expressed by the genome
monomer of a protein/polypeptide amino acid
3 parts of an amino acid amino group, carboxylic group, R group
What makes an amino acid structurally different? the R group
R group of polar amino acids hydrophilic
R group of nonpolar amino acids hydrophobic
number of different amino acids 20
What determines the sequence of amino acids in a polypeptide? genes in DNA
location of the creation of polypeptide chains ribosome
How do monomers create a dipeptide/polypeptides? amino acids bond together
How is a dipeptide / polypeptide is broken down into its monomers? hydrolysis
Primary structure sequence of amino acids, influences all other levels
Secondary structure folding into an alpha helix, beta-pleated sheet or random coil, hydrogen bonds between amino and carboxylic groups
Tertiary structure folding into complex 3D shapes, interactions between side groups
Quaternary structure multiple polypeptides interacting, forms a large single protein
importance of polar and non-polar amino acids in membrane proteins polar amino acids create the inside of the channel where the water is while nonpolar amino acids stay away from water creating the outside of the protein
fibrous proteins thin and thread-like, often play structural roles
globular proteins spherical, play active roles in metabolism
collagen fibrous, maintains structure in connective tissue
spider silk fibrous, makes webs
rubisco globular, fixes CO2 in the Calvin cycle
immunoglobulin globular, creates immune responses
insulin globular, decreases blood sugar levels
rhodopsin globular, helps vision in low light
denaturation of a protein proteins break down when not in optimal conditions, especially temperature or pH level. The hydrogen bonds break and the tertiary and quaternary levels are irreversible changed.
Created by: luciepike
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