7.1 Flashcards

1
Q

Compare and contrast Glutamine and Valine

A

Both have a carboxyl and amino (as they are proteins)

Glutamine has a different side chain compared to Valine, being a basic comapared to Valine being nonpolar.

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2
Q

The four levels of protein structure.

A

Primary - Long chain of amino acids in a certain order. Determined by genes.

Secondary - Regular section of a protein which folds (The area that’s not the side chain). Two types: alpha-helix and beta-pleated-sheet

Tertiary - Interactions between side chains of amino acids in proteins.

Quaternary - Multiple polypeptides bonded.

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3
Q

Protein Denaturation

A

The conditions in which hydrogen or ionic bonds are disrupted, mainly through temperature, but other ways include extreme pH and salinity (salt level).

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4
Q

Tertiary structure interactions.

A

Hydrophobic - Orients towards the inside of the structure

Hydrophilic - Orients towards the outside of the structure.

Basic and Acid - Bond together as bases are positively charged and acids are negatively charged.

Cysteines - Forms disulfide bridges

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5
Q

Protein types (a few)

A

Enzymes - catalyze chemical reactions

Antibodies - prevents infection

Infrastructure - supports and moves cells

Hormones - chemical signal sender

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6
Q

How would the tertiary structure of a protein changed if a hydrophilic amino acid was changed to a hydrophobic amino acid in the primary structure?

A

The tertiary structure will, at a minimum, be slightly different in folding as the new primary structure would fold inwards at the area where the hydrophilic amino acid was. Depending on the fold, it could drastically change the tertiary structure.

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7
Q

Differences between protein denaturation and mutation? (both effects and results)

A

Mutation and denaturation is similar in the fact that they can both heavily affect the tertiary structure of a protein.

The difference is that mutation DOES affect the primary structure (which is why It affects the tertiary structure) while denaturation does not.

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