3.2 and 3.3 Flashcards

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1
Q

macromolecule monomer polymer

A

carbohydrates monomer polysaccarides
lipids fatty acids triglycerides
proteins amino aids polypeptides
nucleic acids nucleotide polynucleotides

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2
Q

macromolecules purpose

A

lipids- chemical messengers and repels water
carbohydrates- energy and structure
Nucleic acids- genetic info
proteins- storage signals structure has enzymes

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3
Q

same and differences in amino acid structure

A

they all start out with the same base but the r group changes the amino acid and changes the folding of it to give it a new function

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4
Q

4 levels of protein structure

A

primary secondary tertiary quaternary

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5
Q

what happens in protein denaturation

A

it breaks the covalent bonds that makes the structure of the protein and the structure becomes deformed

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6
Q

Explain how tertiary structure is formed by interactions between the following:
Hydrophobic interactions
Hydrophilic interactions
Acidic and Basic side chains
Cysteine side chains

A

amino acids with nonpolar, hydrophobic R groups cluster together on the inside of the protein, leaving hydrophilic amino acids on the outside to interact with surrounding water molecules.acid groups whose pKa’s are low enough to lose protons, becoming negatively charged in the process.Their pKa’s are high enough that they tend to bind protons, gaining a positive charge in the process.When a protein folds, two Cys side chains might approach each other, and form an intrachain disulfide bond.

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7
Q

Examples of protein types and functions: i.e. enzymes catalyze chemical reactions

A

Enzymes-catalyst chemical reactions
Hormones-long distance chemical signals
amino acids- monomers that make up the protein
peptide bonds-made up of polypeptide chains

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8
Q

Compare and contrast the structure and functions of different groups of macromolecules

A

Proteins, carbohydrates, lipids, and nucleic acids, are the four major macromolecules. They perform important functions, including providing structural support, being a source of stored fuel, storing and retrieving genetic information, and speeding biochemical reactions.

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9
Q

Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?

A

It can mess with the folding and give the protein an different structure which affects the function

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10
Q

amino acid def

A

molecule the combines to form proteins

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