BIO 200 10/7/2026

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Description and Tags

Proteins - Structure and Function

28 Terms

1
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Polymers are

repeating units of simple monomers that are covalently bonded together

2
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When monomers undergo condensation

covalent bonds are formed between monomers as the hydroxide and hydrogen have their bonds broken from their own respective monomers.

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When polymers undergo hydrolysis

the covalent bonds between the monomers are broken and are hydrogen is attached to one and a hydroxide is attached to another.

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Proteins are polymers of ___ ___ that fold into specific shapes.

amino acids

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Proteins are also referred to as ____ as they contain many peptide bonds.

polypeptides

6
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enzymes typically have names that end with

- ase

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Amino acids are ___ that assemble into proteins

monomers

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Animo acids of proteins have two functional groups:

Amines and carboxylic acid

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Amindo acids are covalently linked together to form a ___ ____

peptide bond - the carboxylic acid looses its oxygen and the anime looses two of its hydrogens during condensation, then the carbon in carboxylic acids bonds with the nitrogen of the anime.

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Amino acids are categorized by the chemical properties of their ___ ___.

side chains (R groups)

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the R group of the animo acids are whats connected to the ___ ___.

central carbon which has the carboxylic acid and anime bonded to it.

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To recognize electrically charged side chains:

Notice on the R-group that there will be an element that has a charge of ±

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To recognize polar side chains on the R-group:

there will be a ± dipole symbol

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To recognize non-polar chain on the R-group:

They’re mainly hydrocarbon and there is no charge on the R-Group.

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There are ___ different amino acids

20

16
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In the lipid memebrane of a cell remember there is a hydrophobic and hydrogphillic area. This means that:

The integral protein is hydrophobic and the peripheral protein is hydrophilic.

17
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There are ____ levels of animo acids

Primary, secondary, tertiary, quanternary

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Primary structure of the order of the animo acids in the polypeptide is described at:

The scale of the primary structure is just the functional groups: animes, carboxylic acid, r-group

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Secondary structure: hydrogen bonding between the non-variable parts of non adjacent animo acids. There are two shapes:

Alpha Helix and Beta Pleated sheet and they’re held together by hydrogen bonds.

20
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Tertiary structure is determined by interactions between __ ___ with each other and the local environment.

side chains

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Quaternary structure involves interactions between different polypeptides to form a ____.

multi-peptide protein

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The process of protein folding is fast and spontaneous and take place as a protein makes these specific ___ ___.

intermolecular interactions

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Methods to denature proteins

changes in temperature, solvent, pH, reducing agent

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Structure ___ function.

Drives - if a protein loses its shape, it loses its function

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Proteins are not ___ structures

rigid - There are constant variations.

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Non polar side chains like hydrocarbons relation to water

hydrophobic and are likely to to cluster on the interior of proteins in water

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side chain that isn’t a hydrocarbon (-OH or -NH2)

hydrophilic polar side chain. Located on the surface of the proteins where they can interact with water.

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Charged side chains like (COO-)

these are charged and generally react with water so they favor the surface of proteins