7.5 Proteins

Question 1

Difference between fibrosis and globular proteins the reference to two examples of each protein l type

Answer 1

Fibrous: shape composed of many polypeptide chains, long narrow shape, insightful to water. Example: collagen and actin

Globular proteins: she is 3-D/round, so I would water. Example: hemoglobin and hormone insulin

Question 2

Explain significance of polar and nonpolar amino acids

Answer 2

Determined by properties R group
-nonpolar = hydrophobic parts of a cell membrane

Polar = hydrophilic parts of the cell, where proteins are exposed to water - interior and exterior or membrane, create hydrophilic Channels in protein through which polar substances can move through

Important: determining the specificity of an enzyme; fitting active site involves polar properties of the substrate and the amino acids exposed to the active site

Question 3

Stay for functions of protein giving a named example of each

Answer 3

Structural: collagen
movement: myosin and actin
enzyme : amalayse (digest starch)
transport: hemoglobin

Question 4

Explain the four levels of protein structure including the significance of each level

Answer 4

primary structure chain of amino acids held by peptide bonds, the order is determined by the nucleotide bases Order in DNA, determines next three levels of protein organization

Secondary: hydrogen bonds between oxygen of amino acid and hydrogen amino acid group of another, does not involve the bonding of our group,, configuration is that helix or beta pleated sheet

Tertiary: bonding of the R groups and peptide backbone creates a 3-D shape, important in determining the specific protein of enzymes301284542

Quaternary: multiple polypeptide chains been together 3-D shape, ex hemoglobin