Biological Molecules Flashcards

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1
Q

Explain dehydration (condensation) reactions as well as hydrolysis reactions in the context of formation and breakdown of biological molecules in cells.

A

dehydration (condensation) reaction - makes polymers by losing water
hydrolysis - breaks down polymers by adding water

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2
Q

Describe the basic building blocks of proteins, as well as their main functional groups and chemical properties

A

monomers (building blocks) - amino acids
main chain - center C, amino group, and carboxyl group (same for every protein)
side chain - R group (unique and results in different amino acids.

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3
Q

What are the functions of proteins?

A

enzymatic, defensive, storage, transport, hormonal, receptor, contractile/motor, structural

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4
Q

What are the amino acid groups and some examples?

A

polar - CO, OH, SH, NH2
nonpolar - CH3, carbon ring
acidic - negatively charged
basic - positively charged

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5
Q

what are amino acids linked by?

A

peptide bonds

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6
Q

what are the 4 levels of folding for proteins?

A

primary, secondary, tertiary, quaternary

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7
Q

Which of the folding structures of proteins intramolecular/intermolecular?

A

intramolecular - primary, tertiary
intermolecular - secondary, tertiary, quaternary

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8
Q

In a cell where pH is normal, what is the amino acid presented as?

A

ionized form - amino group positive charge, carboxyl group negative charge

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9
Q

What is primary folding?

A

amino acids are connected together through peptide bonds

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10
Q

What is secondary folding?

A

main chains interact through hydrogen bonding to form alpha helices and beta sheets

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11
Q

What is tertiary folding?

A

R groups (1 polypeptide) interact based on their classification to form a 3D shape (nonpolar - hydrophobic, polar - hydrogen bonds, acidic/basic - ionic bonds)
2 cysteine amino acid R groups (SH at the end) interact to form covalent bonds

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12
Q

What is quaternary folding?

A

R groups (2 or more polypeptide) interact based on their classification to form a 3D shape (nonpolar - hydrophobic, polar - hydrogen bonds, acidic/basic - ionic bonds)

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13
Q

What is denaturation and the cause of it?

A

protein folds back to its primary structure (no longer biologically active)
cause: change in environmental conditions
ex. change in pH or temp.

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14
Q

What is renaturation?

A

protein goes back to its original structure - denaturation process is reversed, can be done so by reversing environmental conditions that caused the denaturation

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15
Q

What are the 2 types of nucleic acids?

A

DNA, RNA

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16
Q

What is the monomer of nucleic acids and what do they consist of?

A

nucleotide
5-carbon sugar (pentose) - DNA no oxygen, RNA has oxygen
nitrogenous base
phosphate group - create a phosphodiester linkage between 2 nucleotides through condensation reaction)

17
Q

What is a nucleoside?

A

pentose
nitrogenous base
no phosphate group

18
Q

Do proteins contain L or D isomers of amino acids?

A

L-isomers

19
Q

Draw 2 amino acids joined together, identifying the peptide bond and the N and C ends.

A

C (carboxyl) end forms a bond with the N (amino)

20
Q

What are the bases for RNA and DNA?

A

RNA - A-U,C-G
DNA - A-T, C-G

21
Q

What is the sugar present in DNA and RNA

A

DNA - deoxyribose
RNA - ribose