FNDRC NBCD C5 (Proteins) Flashcards by Obret' Calubaquib

The building block of protein is amino acids. What are the groups attached to the carbon of an amino acid?

Hydrogen group
Amino group (NH2)
Acid/Carboxyl group (COOH)

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Yes or No: A protein is made up of about 20 different amino acids, and have the same side group.

NO. Each have different sige group

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A protein is made up of about ___ different amino acids, each with a different side group.

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Amino acids are classfied based on essentiality. There are essential, semi-essential/conditional, and Nonessential.

What are the AAs classified in each group?

ESSENTIAL AA:
1. Phenylalanine
2. Valine
3. Threonine
4. Tryptophan
5. Isoleucine
6. Methionine
7. Histidine
8. Arginine
9. Leucine
10. Lysine

CONDITIONAL
1. Arginine
2. Histidine

NON-ESSENTIAL
1. Aspartate (Aspartic acid)
2. Alanine
3. Glutamine
4. Glycine
5. Cysteine
6. Asparagine
7. Glumate (Glutamic Acid)
8. Tyrosine
9. Proline
10. Serine

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AAs that the human body cannot make at all or cannot make in sufficient quantity to meet its needs.

Essential

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AAs whose rate of synthesis in the body are inadequate to support growth and are therefore needed by young animals.

Conditional

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AAs that can be synthesized in the body in sufficient amounts.

Non essential

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AAs that the body can produce, but under certain conditions—such as illness, stress, trauma, or during infancy—the body cannot produce enough of them, so they must be obtained from the diet.

Conditional

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What do you call the amino acid with one amino group and one carboxyl group?

Neutral Amino Acids

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A type of neutral AA that consists of straight or branched chains of Carbon atoms and other substitutents.

Give examples:

Aliphatic AAs

GAV-LIST
Glycine
Alanine
Valine
Leucine
Isoleucine
Serine
Threonine

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A type of neutral AA that have aromatic rings attached.
Examples?

Aromatic AAs

Phenylalanine, Tyrosine, Tryptophan

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A type of neutral AA that contains sulfur as a subtituent.

Example:

Sulfur-containing amino acids:

Cysteine and Methionine

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A type of neutral AA that contains an additional NH2 (amino) group. GIve example:

Basic Amino Acids
Lysine, Arginine, and Histidine

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A type of neutral AA that contains an additional -COOH (carboxyl) group attached. GIve example:

Acidic Amino Acid
Aspartic and Glutamic

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It is the amino nitrogen that forms part of a ring structure. GIve example:

Imino acid.

Proline and Hydroxyproline

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it is the simplest amino acid

GLYCINE

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These are the amino acids that can be catabolized or broken down to form glucose or glycogen

Glucogenic amino acids

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Glucogenic amino acids can yield what metabolic products?

Tricarboxylic acid cycle components or Pyruvate

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What are the PURELY GLUCOGENIC AAs?

All Silly Girls Can Always Ask Good Guys About His Very Manly Thick Pants

A Alanine
S Serine
G Glycine
C Cysteine
A Aspartic acid
A Asparagine
G Glutamic acid
G Glutamine
A Arginine
H Histidine
V Valine
M Methionine
T Threonine
P Proline

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These are amino acids that can be catabolized to form ketone bodies

Ketogenic AAs

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Ketogenic AAs can yield what metabolic products?

CoA or Acetoacetate

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What are the PURELY KETOGENIC AAs?

Lysine and Leucine

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What are the AAs that are both GlucoAA and KetoAA?

3 aromatics + 1 Aliphatic
AROMATICS: Phenylalanine Tyrosine, Tryptophan
ALIPHATIC: Isoleucine

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It is the ability to form mirror images called D and L forms:

Stereoisomerism

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It is the nature of amino acid that refer to having both the amino and carboxyl group, which can regulate pH.

Amphoteric

This refers to degraded amino acids upon hydrolysis. Give examples:

Simple Proteins: Albumin, Collagen, Elastin, Myosin

These are simple proteins added with a nonprotein. Give examples:

Compound Proteins: Mucoprotein, glycoprotein, and lipoproteins.

These are substances resulting from the decomposition of simple and conjugated proteins. Give examples:

Derived proteins: Peptides, Peptones, and Proteoses

These are coiled or ellipsoidal-shaped amino acids. Give examples:

Globular proteins: Insulin, Albumin, ang Globulin

These are helical peptide chains, GIVE EXAMPLES:

Fibrous proteins: Elastin, Fibrin, and Collagen

A type of protein that contains all the essential amino acids as with the case of all animal proteins except ____.

Complete proteins; gelatin

These contain all the essential amino acids but in limited amounts to support growth. gIve examples:

Partially complete proteins: Gliadin and hordein

These are proteins that lack one or more essential amino acids; cannot maintain life nor support growth. GIve examples:

Zein or Gelatin

Some ____ can be converted to glucose via ____.

Amino acids; gluconeogensis

A sulfur containing AA that is formed from ____ and is abundant in human milk.

Taurine; Methionine.

This protein is needed for retinal and visual function, brain development, and stability of central nervous system activity.

Taurine

This protein is formed from methionine + lysine and converts acyl compound (products of fat metabolism) to less toxic forms and removes them from the cell.

Carnitine

Carnitine is formed from [what AAs] and converts acyl compound (products of fat metabolism) to less toxic forms and removes them from the cell.

methionine + lysine

It is a protein that exerts oncotic pressure for water balance.

Albumin

These are lipid transporters

Lipoproteins

A protein that is involved in immune response

Globulins

A protein that is necessary for blood clotting.

FIbrinogen

Protein for muscle contraction

Actin and myosin

Explain how does protein help in blood pH regulation:

Proteins help regulate blood pH by acting as buffers. This means they can accept or donate hydrogen ions (H⁺) to resist sudden changes in pH. How it works: Proteins, especially albumin and those with amino acid side chains like histidine, contain groups that can bind or release H⁺. When blood is too acidic (too many H⁺), proteins can accept H⁺ to reduce acidity. When blood is too basic (too few H⁺), they can release H⁺ to increase acidity. This buffering action helps maintain the normal blood pH of 7.35–7.45, which is essential for proper body function.

Chemical digestion of protein begins in the _____ with the help of the enzyme _____.

Stomach; Pepsin

________ provides the degree of acidity necessary to convert inactive _______ to its active form _____.

Hydrochloric acid; Pepsinogen ----> Pepsin

Pepsin is produced from what organ and it works in what organ?

From Stomach (chief cells) and works in the Stomach.

An enzyme that breaks proteins into smaller polypeptides; active in acidic pH.

Pepsin

Trypsin and Chymotrypsin is produced from what organ and it works in what organ?

Produced: Pancreas Workplace: Small Intestine (duodenum for trypsin)

This enzyme breaks peptide bonds at the carboxyl side of lysine and arginine (basic AAs)

Trypsin

This enzyme cleaves peptide bonds at aromatic amino acids (e.g., phenylalanine, tyrosine)

Chymotrypsin

This enzyme removes amino acids from the carboxyl end of peptides.

Carboxypeptidase

This enzyme removes amino acids from the amino end of peptides

Aminopeptidase

This enzyme splits dipeptides into individual amino acids

Dipeptidase

Amino acid absoprtion occurs mostly by _______ in the proximal portion of the small intestine.

active transport

Yes or No: Amino acid absorption requires energy and carriers.

Yes. It is absorbed through active transport.

Amino acid absoprtion occurs mostly by ACTIVE TRANSPORT in the proximal portion of the small intestine, requiring carrier, energy and WHAT PARTICULAR NUTRIENTS:

PYRIDOXINE (B6) AND MANGANESE

Maintenance of amino acid pool: Amino acids pass through the portal vein into the liver, which maintains normal levels of amino acid nitrogen in the blood. What is the normal levels? The sources of amino acids in the body can either be:

1.) 4 to 6 mg/dL 2.) exogenous (from dietary protein) or endogenous (from tissue protein breakdown in the body).

This metabolic mechanism involves the incorporation of amino acids in the synthesis of tissue proteins.

Anabolism

ANABOLISM 1. This molecule is present in the cell nucleus and provides the genetic blueprint. 2. The genetic code is carried from the [1] to the site of protein synthesis in the _____ by _____ _______. 3. ________ molecules that are present in the cytoplasm then transport the amino acids based on the code in [2.2]. 4. The _______ is formed through the addition of one amino acid at a time in the ribosomes. 5. When the chain is complete, the ___ is released into the ______.

1. Deoxyribonucleic acid (DNA) 2. ribosome; messenger ribonucleic acid (MRNA) 3. Transfer RNA 4. polypeptide chain 5. protein; cytoplasm 🧩 Analogy: Think of it like building a toy: DNA = the instruction manual mRNA = a copy of the manual sent to the workshop Ribosome = the assembly line tRNA = workers bringing the correct parts (amino acids) Polypeptide chain = the toy being built, piece by piece Protein = the finished toy, ready to be used

This metabolic mechanism which involves the breakdown of amino acids into their component parts.

Catabolism

The breakdown of amino acids results in two components:

1. nitrogenous residue 2. NOn nitrogenous residue/keto-acid residue

In catabolism, the nitrogenous residue (NH2) can undergo what processes:

1. Deamination 2. Transamination 3. formation of other nitrogen-containing compounds (e.g. purines) 4. Formation of Urea

It is the removal of the nitrogen portion to form ____ that is then excreted in the urine. Where does this process occur?

1. Deamination 2. Ammonia 3. Liver or kidneys

This is the transfer of the nitrogenous group to ______ to form another __________.

1. Transamination 2. keto-acid residue 3. Non-Ess AA

This is the chief nitrogenous end product of protein metabolism

Urea

The urea cycle is also known as:

Ornithine

1. In the urea cycle, what are the toxic and non-toxic components to form urea? 2. And what happens after its formation? 3. Where does urea cycle occur? 4. What amino acid is invovled in urea cycle?

1. Blood Ammonia (toxic) + Ornithine (nontoxic) = urea 2. it is being excreted in the urine. 3. Liver 4. Arginine

The carbon skeleton can form either carbohydrates or fat through what Amino acids?

Glucogenic and Ketogenic AAs

FATES OF AMINO ACIDS: Formation of TAG (Triacylglycerol or Fat) in Adipose Tissue 1. When it happens? 2. How it work? 3. Why?

1. If there is excess protein intake, and energy needs are already met. 2. Deamination ➡️ Acetyl-CoA ➡️ Fatty Acids ➡️ FA + Glycerol ➡️ TAG in adipose tissue 3. The body stores extra energy as fat for future use

FATES OF AMINO ACIDS: Formation of Ketone Bodies 1. When it happens? 2. How it work? 3. Why?

1. During fasting, low-carb diets, or uncontrolled diabetes when glucose is low and energy is needed. 2. Ketogenic AAs → Acetyl-CoA (and still low glucose) → Ketone bodies as Alternative energy 3. To fuel the body when carbohydrates aren't available.

FATES OF AMINO ACIDS: Source of Glucose (Gluconeogenesis) 1. When it happens? 2. How it work? 3. Why?

1. During fasting, starvation, or low-carb intake. 2. Glucogenic AAs → Pyruvate/TCA intermediates → Glucose Maintain blood sugar 3. To maintain blood glucose levels when dietary carbs are unavailable.

What do you call the AA that is inadequate in a food item?

Limiting AA

What do you call process in which a protein is paired with another protein, which can supply the lacking AA?

SUPPLEMENTARY PROTEIN

The limiting amino acid in food protein is the amino acid found in short supply relative to need. What is the following food's limiting amino acid? Soybeans and rice

Methionine

The limiting amino acid in food protein is the amino acid found in short supply relative to need. What is the following food's limiting amino acid? Legumes

Methionine and Tryptophan

The limiting amino acid in food protein is the amino acid found in short supply relative to need. What is the following food's limiting amino acid? Green Leafy Vegetables

Methionine

The limiting amino acid in food protein is the amino acid found in short supply relative to need. What is the following food's limiting amino acid? Cereal grains

Lysine and threonine TCL!!!

The nitrogen content of protein is how many percent?

16%

1 g of N = g of dietary protein

1 g N = 6.25 g CHON

In Nitrogen Balance, what is the rule in the following cases? 1. N equilibrium 2. Positive Nitrogen Balance 3. Negative Nitrogen Balance

1. Input = Output 2. Input > Output 3. Input < Output or Output > Input

In what condition of the body does +N balance occur?

Pregnancy, growth, rehabilitation from illness.

In what condition of the body does -N balance occur?

Illness and malnutrition

Total energy requirement of CHON:

10-15%

A safe protein intake level for adults is defined as the:

lowest level of dietary protein intake that will balance the losses of nitrogen from the body in persons maintaining energy balance at modest levels of physical activity

REMEMBER: Ideal protein needs are based on egg/milk (high-quality protein). But since Filipino kids eat mostly rice, which has lower-quality protein, the recommendations are adjusted to match this.

Ideal protein needs are based on egg/milk (high-quality protein). But since Filipino kids eat mostly rice, which has lower-quality protein, the recommendations are adjusted to match this.

Yes or No: Protein rich sources are also high in fat sources that contribute to weight gain.

Yesss

Also known as protien malnutrition/severe protein energy deficiency

Kwashiorkor

Kwashiorkor usually affects what age group?

1-6 y/o

It is also known as non-edematous malnutrition

Marasmus

What are the clinical manifestations of Kwashiorkor?

🌟 Mnemonic: "Big Mama Loves Pretty Apples, Hot Pie, and Ice cream" 1. Bilateral pedal edema 2. Muscle wasting in the gluteal region 3. Loss of subcutaneous fats 4. Prominence of bony structures, particularly over the thorax 5. Appetite loss 6. Pale, thin, peeling skin 7. Hair, sparse 8. Infection

FNDRC NBCD C5 (Proteins) Flashcards

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