Proteins Flashcards
Amino acids
20 kinds, but only 9 are essential amino acids (EAA)
Phenylalanine, valine, tryptophan, methionine, threonine, histidine, isoleucine, leucine, lysine
EAA needs approx. 11% of total protein intake
Typical diet supplies 50% as EAA
Children have higher need for EAA, need high-quality protein in diet
Each amino acid contains
carbon, hydrogen, and nitrogen
“R” group
Specialized side-group
Examples:
Branch-chain amino acids (BCAA) have carbon and hydrogen “R” groups and can be used to make glucose if little or no CHO is consumed in the diet
Leucine, isoleucine, valine
PKU (phenylketonuria) – disease caused by inability to convert “R” group of phenylalanine to form tyrosine
Amino acids are connected via
peptide bonds
Dipeptide
Tripeptide Polypeptide
Denaturation
change in shape
Heat, acid, alkali, agitation can denature
proteins and deactivate them Cooking denatures protein
Makes tough connective tissue softer, easier to chew, swallow, digest
Kills bacteria
Inactivates some biologically active proteins

protein digestion starts…and ends…
Stomach – begins digestion of protein
Acid denatures protein
Pepsin breaks polypeptides into smaller peptides
Small intestine - most protein digestion and absorption occurs here
Pancreatic juice contains proteases which complete digestion of peptides
Single amino acids and some di- and tripeptides are absorbed

Protein turnover
constant synthesis and breakdown of protein
Allows cells to adapt to changes in body circumstances
Amino acids are easily recycled, so we do not need to eat as much protein
If amino acid used for energy, made into glucose, or lost due to cell breakdown, waste product ammonia is produced
Liver turns ammonia into urea which is filtered by kidneys for excretion
protein functions in the body
Structure
Collagen – structural protein
found in bones, skin
Keratin – structural protein found in hair, nails
Acid-base balance
Some proteins act as buffers (resist pH change)
Oncotic pressure
Presence of protein in small blood vessels attract water back into blood, partially counteracting blood pressure
If low protein in diet, too much fluid accumulates in tissues = edema
Hypertension, congestive heart failure, preeclampsia
Fig. 6.9

What affect would a drop in pH (more acidic) have on body proteins?
they would become denatured, this is regulated from happening with the kidney.
Why might an elderly adult with a poor appetite have edema in her feet and ankles?
insufficient protein intake leading to a problem in oncotic pressure, wherein protiens attract water to balance blood pressure. Too much water collects in the ankles causeing swelling.
protein functions in the body (more)
Hormones
Thyroid hormone, insulin, glucagon, growth hormone
Enzymes
Almost all are proteins or contain protein
Immune system
Antibodies are proteins
Energy
If low on CHO, liver and kidneys make glucose from
BCAA
If starving, amino acids can be used for energy muscle and organ wasting
Why does a patient with a poor appetite have a higher risk for infection?
insufficient protein could be part of the problem as antibodies are made of protein.
Why do enzymes and hormones from animal or plant foods not adversely affect our bodies?
This is kind of a loaded question. We know that stomach acid ‘kills’ the zillions of plant and animal based hormones, denatured proteins by acid. However we show that hormones are transfered through breastmilk, and that cooking food denatures enzymes in the foods that are needed to digest.
High-quality/Complete
Source: animal protein
Contains all 9 essential amino acids
Lower-quality/Incomplete
Source: plant protein
Missing at least 1 essential
amino acid
Limiting amino acid = essential amino acid missing from protein food or in body
Complementary protein = plant protein that contains limiting amino acid of another plant protein