Chapter 7: Proteins and Amino Acids (Oct 15 lec) Flashcards

1
Q

Why is it that herbivores can digest animal protein and carnivores can digest animal protein?

A

both plant and animal proteins are made up of the same 20 amino acids
- same bonds and structural themes, different amino acid profiles

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2
Q

peptides=

A

chains of amino acids joined by peptide bonds

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3
Q

proteins and polypeptides

A

both are chains of amino acids joined by peptide bonds

  • polypeptides= a long chain
  • proteins= an even longer chain
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4
Q

Water is ___ when a peptide bond is formed. Is this process reversible?

A

lost

Yes! water molecule required to break down peptide bonds

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5
Q

primary protein structure

A

a sequence of a chain of amino acids

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6
Q

secondary protein structure

A

h-bonding of the peptide backbone causes the amino acids to fold in a repeating pattern
- alpha helix or pleated beta sheet

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7
Q

tertiary protein structure

A

3D folding pattern of a protein due to side chain interactions

  • lowest energy configuration spontaneously forms
  • this tertiary structure can be the fully functional protein
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8
Q

quaternary protein structure

A

protein consisting of more than 1 amino acid (polypeptide) chain

  • tertiary not always fully functional by themselves, but when put together it’s functional
  • compact structure limits where enzymes can be active (hard to get peptide bonds to break them)
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9
Q

How does cooking denature protein?

A

disrupts the tertiary structure- protein folding

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10
Q

T/F

cooking is necessary for the digestion of protein

A

false- it’s possible to digest protein that’s not denatured

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11
Q

a denatured protein is

A

more stretched out, more susceptible to enzyme degradation

- allows access to peptide bonds by pepsin in stomach

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12
Q

If ingested protein is not denatured, it is denatured in the ___ by ____

A
stomach
HCl (does not break down the protein itself, just denatures it)
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13
Q

zymogen=

A

an inactive precursor of an enzyme

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14
Q

peptidase/ protease=

A

an enzyme that catalyzes the breakdown of proteins

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15
Q

In the small intestine and pancreas, pH is near ____ and peptidases are secreted by _____

A

neutral

zymogens

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16
Q

Trypsin is an enzyme that aids with ____. _____is the precursor of trypsin and is stored in the ___.

A

digestion

Trypsinogen
pancreas

17
Q

How does trypsinogen get activated into trypsin?

A

Enterokinase (an enzyme secreted by mucus in the intestine) cleaves trypsinogen to trypsin.
Once active, trypsin can go back and activate trypsinogen and other zymogens

18
Q

match the terms

  • Enterokinase, trypsin, trypsinogen
  • active enzyme, cleaving enzyme, zymogen
A

cleaving enzyme= enterokinase

zymogen= trypsinogen

active enzyme= trypsin

19
Q

why are proteins secreted as proteins?

A

To prevent the enzymes from digesting proteins in the cells in which they’re synthesized (b/c it’s an inactive precursor)

20
Q

What do endopeptidases do?

Where do they work?

A

takes a long chain and chops it up into shorter chains (not yet amino acids)
more chains= more carboxy ends for exopeptidases to work

small intestine

21
Q

What do exopeptidases do?

A

hydrolyze the ends of a chain (either carboxy or amino end)

  • carboxypeptidase
  • aminopeptidase
22
Q

T/F
active enzymes cleave specific peptide bonds.

Give ex

A

true

ex. Chymotrypsin –> basic amino acids

23
Q

Why does the intestine block absorption of intact protein?

A

the immune system would go crazy… reacting to foreign protein (lots of things that can hurt us are proteins, so the body attacks it)

24
Q

exceptions: when can the body absorb intact proteins?

A
  1. newborns: first 24hrs after birth (gut closes to intact proteins after this)
    - purpose= passive immunity
  2. Adults:
    - paracellular routes- tight junctions b/w cells (leaky gut)