Chapter 1- Proteins Flashcards

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1
Q

Proteins

A

contain C, H, O, N atoms (CHON)

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2
Q

Amino acids

A

are the monomers of proteins.
Contain Amino, Carboxyl, R-group, and Hydrogen atom.
20 amino acids with different R-groups.

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3
Q

Polypeptides

A

made up of amino acids (forms proteins)

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4
Q

Proteome

A

all of the proteins in a single cell. Can vary from cell to cell

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5
Q

Polypeptides

A

polymers of amino acids joined by peptide bonds.

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6
Q

Dehydration in polypeptides

A

is what forms peptide bonds and polypeptides

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7
Q

Hydrolysis in polypepetides

A

break peptide bonds

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8
Q

N-terminus (amino terminus)

A

side of polypeptide that ends with amino group

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9
Q

C-terminus (carboxyl terminus)

A

side of polypeptide that ends with carboxyl group

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10
Q

Primary structure of protein

A

sequence of a peptide determined by DNA.

All proteins have primary structure

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11
Q

Secondary structure

A

contains a-helix and B-pleated sheet.

hydrogen bonding between polypeptide backbones (no R-groups)

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12
Q

Tertiary Structure

A

3-D folding structure due to side chain interactions.

hydrophobic or hydrophilic spaces depending on R-groups.

Disulfide bonds are created by covalent bonding between R-groups of 2 cysteine amino acids.

Usually not covalent except for when there is disulfide bond

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13
Q

Hydrophobic

A

water-hating/nonpolar

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14
Q

Hydrophilic

A

water-loving/polar

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15
Q

Disulfide bonds

A

very strong bonds that act to hold tertiary structure pf polypeptide.

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16
Q

Cysteine

A

contains Sulfur (S) which allows for disulfide bonding in 3 structure

17
Q

Quaternary structure

A

large proteins containing multiple polypeptide chains.

18
Q

Tetramer protein

A

Has four subunits: primary, secondary, tertiary, quaternary

ex: hemoglobin

19
Q

Globular protein

A

spherical caused by tightly folded polypeptide chains.
Usually hydrophilic (water soluble)
ex: hemoglobin, myoglobin

20
Q

Fibrous protein

A

elongated providing structure support. hydrophobic on the outside making the water non-soluble

21
Q

Proteins classified based on structure and composition

A

Structure: fibrous, globular, intermediate
Composition: can be simple (amino acids) or conjugated ( amino acids + other component)

22
Q

Protein denaturation

A

the loss of protein function and structure.

Can denature by:
high or low temperature, ph changes, salt concentrations,
radiation

Only primary structure remains unaffected.

23
Q

Cooking an egg in high heat disrupts IMF in egg’s protein causing it to coagulate, this is an example of

A

protein denaturation

24
Q

Genome

A

All the DNA in a cell

25
Q

Cysteine

A

Amino acid that Contains sulfur (S)

form covalent bonding

Can create disulfide bonds that are very strong