Chapter 7 Proteins

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56 Terms

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What elements make up a protein?

Carbon, hydrogen, oxygen, and nitrogen

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What are the building blocks (monomers) of proteins?

Amino acids

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What are the parts of an amino acid?

Central carbon, hydrogen, amino group (NH₂), carboxyl group (COOH), and an R-group (side chain)

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What makes each amino acid unique?

Its R-group (side chain)

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How many amino acids are there total?

20

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How many amino acids are essential?

9 (must get from diet)

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How many are nonessential?

11 (body can make them)

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What are “conditionally essential” amino acids?

Nonessential AAs that become essential during stress, illness, or infancy

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What is a peptide bond?

The bond between two amino acids formed via a condensation reaction

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What is a polypeptide?

A chain of 10+ amino acids

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List the 4 levels of protein structure.

  1. Primary – sequence of amino acids; 2. Secondary – coils & sheets from H-bonding; 3. Tertiary – 3D folding; 4. Quaternary – 2+ polypeptides
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What is protein denaturation?

Loss of structure/function from heat, acid, salt, agitation

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Where does protein digestion begin?

Stomach

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What hormone triggers protein digestion?

Gastrin – stimulates HCl & pepsinogen

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What does HCl do in protein digestion?

Denatures protein and activates pepsin

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What does pepsin do?

Breaks large proteins into polypeptides & amino acids

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What enzyme is released in the small intestine?

Proteases from the pancreas: Trypsin, chymotrypsin, carboxypeptidase

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What enzymes are in the brush border?

Aminopeptidase, Dipeptidase, Tripeptidase

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What is the final end-product of digestion?

Free amino acids

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How are amino acids absorbed?

Active transport into enterocytes, then into bloodstream → liver

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What is protein turnover?

Ongoing breakdown & resynthesis of body proteins

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What are the steps of protein synthesis?

  1. Transcription – DNA → mRNA; 2. Translation – mRNA → protein
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What happens if the DNA sequence is wrong?

Protein may be abnormal (ex: sickle cell hemoglobin)

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What is deamination?

Removal of the amino group (NH₂) forming ammonia (NH₃)

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What happens to ammonia in the body?

Converted to urea, filtered by kidneys, excreted in urine

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What is transamination?

Transfer of amino group to make a new nonessential amino acid

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What is gluconeogenesis?

Making glucose from amino acids

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Name 5 functions of proteins.

  1. Structural – collagen, muscles; 2. Enzymes; 3. Hormones; 4. Transport; 5. Immune – antibodies
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What does protein do for fluid balance?

Prevents edema by pulling fluid into blood vessels

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How does protein affect pH balance?

Acts as a buffer to prevent acidosis or alkalosis

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What is protein sparing?

Using carbs & fats for energy, saving protein for body functions

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What is the RDA for protein?

0.8 g/kg body weight (for healthy adults)

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What is nitrogen balance?

Positive – building tissue; Negative – breaking down tissue; Zero – equal intake & excretion

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What makes a high-quality protein?

Contains all 9 essential AAs, highly digestible

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What are complementary proteins?

Two plant proteins that together provide all essential amino acids (ex: rice + beans)

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What is kwashiorkor?

Protein deficiency → edema, brittle hair, skin issues

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What is marasmus?

Overall starvation → severe weight loss & wasting

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What is marasmic-kwashiorkor?

Combo of both – edema plus severe muscle/fat loss

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What conditions may result from too much protein?

Kidney strain, kidney stones, osteoporosis, heart disease

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What causes food allergies?

Immune system reacts to proteins as foreign invaders

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What is anaphylaxis?

Life-threatening allergic reaction → drop in blood pressure, difficulty breathing

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What is celiac disease?

Autoimmune reaction to gluten → damages intestinal villi

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What is PKU (Phenylketonuria)?

Genetic disorder → can’t convert phenylalanine to tyrosine, leads to brain damage if untreated

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The health professional who will consider genetically driven dietary recommendations when helping people with their personalized nutrition plan is the ….

registered dietitian nutrionist

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Every cell contians protein.

True

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A food intolerance may occur after the consumption of nonprotein substances, such as:

Lactose, MSG, and short chain fermentable carbs

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Where are dipeptides and tripeptides broken into amino acids?

Microvilli

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Making dietary choices based on nutritional genomics, height, weight and health assessment is the concept of….

Personalized nutrition

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Intolerance to wheat products, resulting in IBS-like symptoms is defined as….

non-celiac glutern sensitivity

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There are….nonessential amino acids

11

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What happens to peptides once they enter the absorptive cells?

They are broken down into amino acids.

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After proteins are digested, most of the resulting amino acids are….

transported into absorptive cells

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To determine a person's RDA for protein, multiply his or her weight in kilograms by….grams

0.8

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A high-protein diet is defined as a protein intake of….of calories

20-35%

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Following the digestion of proteins, most amino acids are first transported into….

Absorptive cells

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