7.1 Flashcards
What is similar and different between every amino acid?
The side chains, or r groups, are different for each amino acid, but all amino acids have a central carbon, hydrogen, carboxyl group, and amino group.
What makes the amino acids polar, nonpolar, basic, or acidic?
Hydroxyl and carbonyl groups in side chains make amino acids polar, a side chain having primarily hydrogen and carbon makes an amino acid nonpolar. Carboxyl groups in side chains make amino acids acidic, and nitrogen and hydrogen make amino acids basic.
What are the four levels of protein structure?
Primary structure is the sequence of amino acids in the protein. Secondary structures are helixes or pleated sheets. Tertiary structures are made up of some secondary structures and their overall shape is determined by how the amino acids affect each other. Quaternary structures are made up of multiple polypeptides; not all proteins have a quaternary structure.
How do interactions between amino acids form tertiary structures?
hydrophobic groups stay near the middle of the structure to stay away from water, cysteine forms disulfide bonds, acidic and basic groups are attracted to each other, and polar molecules stay to the outside of the structure, near the water.
What happens during protein denaturation?
A protein is unfolded from its complicated shape because of heat, pH, or salinity. It can happen to everything except the primary structure, since the primary structure is what the protein is unraveled down to.
What proteins have which functions?
Infrastructure proteins support things and enable movement. Enzymes make chemical reactions. Hormones control the levels of different things in the bloodstream. Viruses invade other things. Antibodies defend against viruses and harmful bacteria. Channels, pumps and receptors communicate messages and transport nutrients.
How would the structure of a protein change if a hydrophobic amino acid was replaced by a hydrophilic one?
The hydrophilic one would move from the inside of the protein to the outside, close to the water, drastically changing the shape of the protein since part of what was the inside is now facing outwards.
How are the effects and results of protein denaturation different from those of a mutation?
Protein denaturation make the protein unable to do anything at all, a protein can still slightly function with a mutation.
