bio sci 93 - lecture 4: macromolecules ii: proteins & nucleic acids

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Last updated 5:54 AM on 10/13/26
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30 Terms

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describe structural characteristics and functions of proteins. Identify different types of amino acids (polar, nonpolar, charged)

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discriminate and compare the different levels of protein organization. estimate the consequence of alterations in protein structure according to the organizational level involved

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predict the functional consequences of “single base change in DNA → single base change in mRNA → single AA change in protein

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justify the role of chaperone proteins in cells, their location and mechanism of action

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justify the role of proteasomes in cells, their location and function

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describe structural characteristics and functions of nucleic acids. identify different types of nucleotides, recognize nucleotide components. compare and contrast DNA and RNA structure and function. solve basic problems of DNA/RNA structure

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compare the complexity of the genome vs proteome

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protein function:

support, storage, transport, signaling, receptors, movement, catalysis, defense

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protein structure:

amino acids - monomers, combine to form polymers

polypeptide - polymer of AAs in specific sequence

protein - one or more polypeptides w/ specific 3-d conformation

amino acids —> polypeptides —> proteins

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proteins are all constructed from…

same set of 20 amino acids

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structure of amino acid

1) amino group

2) hydrogen

3) carboxyl group

4) R group: variable side chain

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nonpolar

hydrophobic

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polar

hydrophilic

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charged

hydrophilic

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amino and carboxylic acid groups are in ionized form (as in a cell)

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formation of polypeptide

amino end, carboxy end

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three levels of structure in a single polypeptide that organize the folding:

primary, secondary, tertiary, quaternary

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primary structure

determined by AA sequence

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secondary structure

alpha helix (coils), beta pleated sheets (folds)

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tertiary structure

R group interactions

weak: hydrogen bonds, ionic bonds, hydrophobic, van der Waals interactions

strong: covalent bond

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quaternary structure

overall protein structure resulting from combined polypeptides: 2 or more

stabilized by R group interactions

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the effect of a single change in primary structure can have pleiotropic consequences

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carbohydrates, proteins, nucleic acids

polymer: long molecule built from similar subunits (monomers) linked by covalent bonds

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lipids (not polymer)

diverse group of hydrophobic macromolecules

built from two or more different types of smaller subunits

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nucleic acid function

store and transmit hereditary information

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nucleic acid structure

polymers of nucleotide monomers

nucleotide monomers: pentose sugar, nitrogen base, phosphate group

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two types of nucleic acids:

DNA & RNA

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DNA

double stranded

C G A T

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RNA

single stranded

C G A U

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polynucleotides (nucleic acid polymer)

sugar connected to phosphate group of adjacent nucleotide

backbone: sugar-phosphate unit

side chains: nitrogen bases