proteins Flashcards

1
Q

amino acids

A

the building blocks of protein

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2
Q

how many different amino acids are there?

A

20

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3
Q

what is another name for ampholyte/amphoteric?

A

zwitterion

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4
Q

polypepetide chain

A

protein chain of less than 40-50 amino acids

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5
Q

what is another name for polypeptide chains?

A

residues

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6
Q

when does a polypeptide become a protein?

A

when there are 40-50 or more polypeptides

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7
Q

what kind of bond are peptide bonds?

A

covalent bonds

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8
Q

peptide bond characteristics

A

partial double bond, uncharged but polar

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9
Q

what type of isomer does fatty acids favor (cis/trans)?

A

cis favored

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10
Q

what type of isomer does amino acids favor (cis/trans)?

A

trans favored

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11
Q

primary structure of proteins

A

peptide bonds, connect 1 amino acid to another, short + no rotation

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12
Q

secondary structure of proteins

A

regular repeating local structures. stabilized by hydrogen bonds. contain alpha-helix, beta-sheets + triple-helix

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13
Q

tertiary structure of proteins

A

3-D structure formed by assembly of secondary structures

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14
Q

quaternary structure of proteins

A

structure formed by more than 1 polypeptide chain. contains all bonds

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15
Q

primary structure characteristics

A

sequence of amino acids. written left to right. starts with n-terminal amino acid + ends with c-terminal amino acid

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16
Q

secondary structure characteristics

A

organized compact structure of primary proteins

17
Q

alpha-helix

A

spiral structure, tightly packed, polypeptide backbone, high tensile strength

18
Q

beta-sheets

A

polypeptide chain arranged side by side, hydrogen bonds, fibrous protein, pleated look, parallel/antiparallel structure

19
Q

triple-helix

A

3 polypeptide chains woven, hydrogen bonds

20
Q

examples of triple-helix

A

collagen! glycine, proline, hydroxyproline, hydroxylysine

21
Q

tertiary structure

A

cross links between R groups of secondary amino acids in chain

22
Q

quaternary structure

A

folded proteins bind together to form dimer/trimers. 4 polypeptide chains

23
Q

what is the functional form of hemoglobin (quaternary structure)?

A

tetramer

24
Q

what are the bonds of the backbone + side chains of proteins?

A

covalent bonds

25
Q

what bond maintains secondary, tertiary, + quaternary structures?

A

non-covalent bonds

26
Q

hydrophobic AA

A

residues cluster in interior of globular proteins

27
Q

hydrophilic AA

A

face the interior of a structure or away from water

28
Q

chaperones

A

proteins that assist the non-covalent folding/unfolding and the assembly/disassembly of other macromolecular structures

29
Q

protein turnover

A

constant synthesizing/degrading, allowing removal of abnormal or unneeded proteins

30
Q

ubiquitin-protease mechanism

A

proteins synthesized in the cell

31
Q

degradative enzymes

A

acid hydrolases of the lysosomes

32
Q

denaturation

A

disruption of secondary, tertiary, + quaternary proteins by heat/organics, acids/bases, heavy metal ions, + agitation