3.2 and 3.3 Flashcards
Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?
Would cause the folds to change and the protein could not fit in a substrate, which for example, could cause cells to divide faster.
What happens during protein denaturation
It unfolds the protein.
With conditions that disrupt H bonds and ionic bonds that can be temp, pH or salinity.
What are the four levels of protein structure?
Primary Structure
Secondary Structures
Tertiary Structure
Quaternary Structure
What are the monomers of Carbohydrates, Lipids, Proteins, and Nucleic Acids?
Monosaccharides
Fatty Acids
Amino Acids
Nucleotides
What are the polymers for Carbohydrates, Lipids, Proteins and Nucleic Acids?
Polysaccharides
Triglycerides or Phospholipids
Polypeptide
DNA or RNA
What is the significance of enzymes in sugar digestion?
They break down the polysaccharides into monosaccharides so they can be used.
In Lipids, where does the energy come from?
Hydrocarbons
What is the basic phospholipid?
A hydrophilic head and hydrophobic tail
How is the tertiary structure formed with Cysteine side chains, Hydrophobic/ Hydrophilic and Acidic and Basic side chains?
Cysteine: Fold inside, Covalent
Hydrophobic: Clump together, and fold inside.
Hydrophilic: On the outside forming hydrogen bonds
Acidic and Basic: Ionic, on the outside.
Hydrophobic clump to the middle while Polar form hydrogen bonds together.
What are the similarities/differences in amino acid structures?
Similarities: Amino and Carboxyl Functional group. Include a side chains known as a “R group”
Differences: The “R group” includes different functional groups.
