AMINO ACIDS AND PROTEINS Flashcards by Unknown Unknown

Building blocks of more complex compounds

Amino acid

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Amino acids Have three parts

Amino group, Side chain or R group, carboxylic acid group

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The carbon at the center

Alpha - carbon

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Their R groups are mostly hydrogen
and carbon

○ Non-polar hydrophobic

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Their R groups are alcohol, phenol,
thiol, amide

polar and charged

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Their R group can’t be seen but
supposedly, the oxygen has a
negative charge

polar acidic

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The negative charge of the oxygen
are one of the signs that describes
the amino acid as __________

polar acidic

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Instead of having a negative charge,
a positive charge can be seen its side
chains

polar basic

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sential Amino Acids
- It is required in the diet but cannot be synthesized in the body

essential amino acid

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give me the essential amino acid

P-phenylalanine
V - valine
T - Threonine

T-Trytophan
I - Isoleucine
M - methionine

H - histidine
A - arginine
L - leucine
L - lysine

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Not required in the diet but can be synthesized by the body

Non-essential amino acid

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Give me the 12 non-essential amino acid

Alanine
● Asparagine
● Aspartic Acid
● Cysteine
● Glutamic Acid
● Cysteine
● Glutamic Acid
● Glutamine
● Glycine
● Proline
● Serine
● Tyrosine

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Ala

Alanine

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Arg

Arginine

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Asp

Aspartic acid

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Asn

Asparagine

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cys

Cysteine

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Gln

Glutamine

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Glu

Glutamic Acid

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Gly

Glycine

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His

Histidine

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IIe

Isoleucine

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Leu

Leucine

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Lys

Lysine

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Met

Methionine

Phe

Phenylalanine

Pro

Proline

Ser

Serine

Thr

Threonine

Trp

Tryptophan

Tyr

Tyrosine

Val

Valine

Sec

Selenocysteine

Pyl

Pyrrolysine

● Plays a role in cell division

Arginine

● Plays a role in cell division

Arginine

Healing of wounds, stimulation of protein synthesis ● Immune function

Arginine

Release of hormones

Arginine

Required for the generation of urea and synthesis of creatin

Arginine

is the less toxic form produced from the ammonia metabolized in the urea cycle

Urea

is a compound involved in the supply of energy for muscle contraction

Creatin

is synthesized with arginine

Creatine

when broken down forms creatinine

Creatinine

● Direct precursor of histamine

Histidine

● Repair body tissues

histidine

● Maintain myelin sheaths that protect the nerve cells

histidine

Helps manufacture RBC and WBC

histidine

● Protect the body from heavy metal toxicity

histidine

Needed for hemoglobin formation

Isoleucine

Helps to regulate blood and glucose levels and maintain energy levels

Isoleucine

Boosts healing of muscle, skin, and bones

Leucine

Optimal growth of infants and for nitrogen balance in adults

Leucine

● Lowers blood glucose levels

Leucine

Plays a role in the production of antibodies and antibodies (immunoglobulins) and lowers triglyceride levels

Lysine

Needed for proper growth and bone development in children and to maintain a proper nitrogen balance in adults

Lysine

Helps in the absorption of calcium and the formation of collagen

Lysine

Helps initiate translation of messenger RNA

Methionine

First amino acid encoded during translation

Methionine

If __________is not encoded, translation won’t happen

methionine

The codon that encodes for methionine is the start codon, ________

AUG

Source sulfur

Methionine

functions for the normal metabolism and growth of the body

sulfur - methionine

● Assist the breakdown of fats

methionine

● Helps to detoxify lead and other heavy metals

methionine

● Helps diminish muscle weakness

methionine

● Prevents brittle hair

methionine

Promotes alertness and vitality, elevates mood, decreases pain, aids memory and learning

phenylalanine

● Used to treat arthritis and depression

phenylalanine

phenylalanine Used by brain to produce _______

norepinephrine

Uses active transport channel to cross the BBB

Phenylalanine

BBB

blood brain barrier

Interferes with the production of serotonin

phenylalanine

Part of the composition of aspartame

phenylalanine

Common sweetener in (?) food as sugar replacment

aspartame

Important in the component in the formation of protein, collagen, elastin, and tooth enamel

threonine

Helps maintain proper protein balance and aids in liver function, metabolism, and assimilation

threonine

Precursor for serotonin (5-hydroxytryptamine) and melatonin

trytophan

■ Stabilized the mood

Serotonin

■ Person feeling happy

Serotonin

Hormone secreted by pineal gland

melatonin

Sleep week cycle (highest during night time

melatonin

● Natural relaxant

trytophan

Alleviate insomnia by inducing sleep, soothes anxiety and reduces depression

trytophan

● Used in treatment of migraine headaches

trytophan

● Aids in weight control by reducing appetite

trytophan

● Helps control hyperactivity in children

trytophan

● Heaviest among all the amino acids

trytophan

Needed for muscle metabolism and coordination, tissue repair, maintenance of nitrogen balance

valine

● Used by muscle tissue as an energy source

valine

Used in treatments for muscle, mental and emotional problems (insomnia, anxiety, liver and gallbladder disease)

valine

Involved in the breakdown of glucose

Alanine

● Product of the breakdown of DNA

Alanine

● Transfer of nitrogen from the peripheral tissue to the liver

alanine

Helps in reducing the buildup of toxic substances that are released into muscle

alanine

Strengthens the immune system through production of antibodies

alanine

● First amino acid to be isolated

asparagine

● From asparagus juice

asparagine

Converting one amino acid into another via amination and transamination

asparagine

Amine group is introduced to an organic molecule

Amination

Amino acid is transferred to an alpha keto acid (alpha ketoglutarate)

Transamination

Required by the nervous system and synthesis of ammonia

Asparagine

A metabolite in the urea cycle and participates in gluconeogenesis

Aspartic acid

● Named after cystine (precursor)

Cysteine

will travel in your cells, and as it goes inside the cells, it will be reduced to 2 cysteine molecules

cystine

● Also known as half-cystine residue

cysteine

● Production of flavors

cysteine

● Contains sulfur

cysteine

Serves as a neurotransmitter and dysregulation has been linked to epileptic seizures

Glutamic acid

● aids in transporting potassium to the spinal fluid

Glutamic acid

● responsible for the taste umami

Glutamic acid

food additive/food enhancer(sodium salt, monosodium glutamate (bitsin)

Glutamic acid

● most abundant amino acid in the body

Glutamine

assists in maintaining the proper acid/alkaline balance in the body (regulates pH)

Glutamine

supplement used for muscle growth in weightlifting and bodybuilding

Glutamine

transports ammonia to the liver

Glutamine

is toxic to the body (increased levels is dangerous), may lead to comatose

ammonia

● Simplest amino acid

Glycine

One element in the side chain

no stereoisomer

only amino acid not optically active because it has no stereoisomers

Glycine

● has a sweet taste and is used as a sweetener

glycine

● Inhibitory neurotransmitter in the cns

glycine

helps in the synthesis of bile acids

glycine

retards muscle degeneration, improves glycogen storage and promotes healing

glycine

precursor of hydroxyproline

Proline

Technically not an amino acid, but an imino acid

proline

role in wound healing and molecular recognition

Proline

● works with vit. c to promote healthy connective tissues

Proline

technically not a protein since it is an imino acid due to its cyclic structure

proline

needed for proper metabolism of fats and fatty acids

serine

● highly concentrated in all cell membranes

serine

● Component of the protective myelin sheaths surrounding nerve fibers

serine

precursor of epinephrine, norepinephrine, dopamine, t3 and t4

Tyrosine

_______are thyroid hormones

Tyrosine

● stimulates metabolism

Tyrosine

mood elevator, suppresses appetite and helps reduce body fat

tyrosine

treatment of chronic fatigue, narcolepsy, anxiety, depression, low sex drive, allergies and headaches

tyrosine

TWO NEW AMINO ACIDS (established 2002

Selenocysteine Pyrrolysine

encoded by uga codon

selenocysteine

- a sulfur in cysteine is replaced by selenium

selenium analogue

● found in some enzymes

Formate dehydrogenase ○ Glycine reductase ○ And some hydrogenases

main bile acid in the body:

folic acid and chenodeoxycholic acid

main bile acid in the body:

folic acid and chenodeoxycholic acid

Encoded by UAG codon

Pyrrolysine

● Used by archaea and unicellular organisms

Pyrrolysine

product of ketogenesis

acetoacetyl coa and Acetyl coa

Can be (?) in the metabolic pathway ketogenesis

Acetoacetyl coa

can enter ketogenesis or will be allowed to enter the citric acid cycle

acetyl coa

Can generate precursor of glucose: Pyruvate→ gluconeogenesis or create Acetyl CoA and enter citric acid cycle

Glucogenic

○ Process of removing amino group

● Oxidative deamination or Transamination

alpha keto glutamate ● Will enter common metabolic pathway

keto acid

Toxic to the body and should be converted to less toxic form

UREA

Toxic to the body and should be converted to less toxic form

Ammonia

Rare, inherited disorders of aminoacid metabolism

AMINOACIDOPATHIES

Abnormalities in activity of a specific enzyme in the metabolic pathway

AMINOACIDOPATHIES

Abnormalities in the membrane transport system for amino acids

AMINOACIDOPATHIES

● Brought about by genetic defect.

AMINOACIDOPATHIES

● autosomal recessive trait

PHENYLKETONURIA (PKU)

Must inherit 2 mutated gene one from each parent

PHENYLKETONURIA (PKU)

● Total absence of activity of PHENYLALANINE

PHENYLKETONURIA (PKU)

Catalyzes the conversion of phenylalanine to tyrosine

HYDROXYLASE

if there's accumulation in the blood

hyperphenylalaninemia

If the phenylalanine is present in the urine

phenylketonuria

Occurs as a result of the toxic effects of the brain of phenylpyruvate or one of its metabolic by-products

Retarded mental development - 2nd or 3rd week of life - expect microcephaly

deamination of phenylalanine

Phenylpyruvate

decarboxylation and oxidation of phenylpyruvate

Phenylacetic acid

glutamine conjugate of phenylacetate

Phenylacetylglutamine

If the mother has phenylketonuria and the baby kay wala, maagapan mo na ma experience ng baby ang phenylketonuria

Make sure that the mother will undergo phenylalanine restricted diet

Spores of Bacillus subtilis are incorporated into an agar plate that contains beta-2- thienylalanine (antagonist)

Guthrie Bacterial Inhibition Assay

● Filter paper disk impregnated with blood from the infant is placed on the agar mg/dL, phenylalanine counteracts the antagonist and bacterial growth occurs

Guthrie Bacterial Inhibition Assay

if may bacterial growth around the disc

Positive

if walang growth

Negative

Allow the extract to react with the microtiter plate which contains ninhydrin, succinate, leucylalanine, and copper tartrat

Microfluorometric assay

direct measurement of phenylalanine in dried blood filter disks

Microfluorometric assay

Based on the fluorescence of a complex formed of phenylalanine-ninhydrin-copper in the presence of a dipeptide (Lleucyl-L-alanine

Microfluorometric assay

● Excitation/emission wavelengths of 360 nm and 530 nm respectively

Microfluorometric assay

Positive blood test results: bacterial halo =

PKU

Negative controls

no bacterial growth

Positive controls

increasing phenylalanine

Reference method/standard method

High-Performance Liquid Chromatography (HPLC)

is one of the diseases that is tested in newborn screening

PKU

monitoring

Urine test

nvolves the reaction of ferric chloride with phenylpyruvic acid (possible analyte present) in urine to produce a

green color

Involves the reaction of ferric chloride with phenylpyruvic acid (possible analyte present) in urine to produce a green color

Reagent strip test

Characterized by excretion of tyrosine and tyrosine catabolites in urine

Tyrosinemia

■ Most severe ■ Possible symptoms: failure to thrive

Fumarylacetoacetate (FAA) hydrolase (type I)

new born in HPLC

1.2 – 3.4 mg/dL (70-200 umol/L)

scarring of liver tissue

Cirrhosis

Autosomal recessive disorder

Alkaptonuria

an arthritis-like degeneration

Ochronosis

Also tested in newborn screen

Maple Syrup Urine Disease

Autosomal recessive genetic disorder

Maple Syrup Urine Disease

Maple syrup urine disease : Blocking the normal metabolism of

Leu, Ile and Val

Maple syrup urine disease: Modified Guthrie test:

4-azaleucine

MPSUD : Microfluorometric assay

Leucine dehydrogenase above 4 mg/dL is indicative of MSUD

Complications of MSUD

lethargy, failure to thrive, muscle rigidity, respiratory irregularities, mental retardation, comvulsions, acidosis, hypoglycemia

Deficiency of isovaleryl-CoA dehydrogenase in leucine pathway

Isovaleric Acidemia

“sweaty feet” odor

Isovaleric acidemia

● Perform chromatography

Isovaleric acidemia

Increased levels of homocysteine

Homocystinuria

Intermediate amino acid in the synthesis of cysteine from methionine

Homocysteine

Impaired activity of cystathionine beta-synthase (homocysteine to cysteine)

homocystinuria

Cysteine and homocysteine are reduced by sodium cyanide to free-thiol

● Cyanide-Nitroprusside Urine Spot Test

Results from inherited enzyme deficiencies in the urea cycle

Citrullinemia

○ Then, reacted to sodium nitroprusside to produce a red-purple colo

Cyanide-Nitroprusside Urine Spot Test

Silver nitrate reduces homocysteine to form reddish color

Silver-nitroprusside Test

COMPLICATIONS OF SILVER NITROPRUSSIDE TEST

COMPLICATIONS: ○ Thromboembolism, Cardiovascular risk, Atherosclerotic disease, Low folate concentrations, Vitamin B12 deficienc

lack of the enzyme argininosuccinic acid synthetase (ASS)

type 1 OF CITRULLINEMIA

caused by a mutation of the gene that would provide instructions for making the protein citrin

Type 2

helps transport molecules inside cells that used to produce simple sugars, proteins, nucleotides, and molecules used in the urea cycle

citrin

Citrullinemia complications

Vomiting, high ammonia levels and Mental retardation may lead to comatose

Results from inherited enzyme deficiencies in the urea cycle

Argininosuccinic Aciduria

● Deficiency in argininosuccinate lyase (ASL)

Argininosuccinic aciduria

a defect in the amino acid transport system rather than a metabolic enzyme deficiency

Cystinuria

■ Insoluble ■ Tends to precipitate in the kidney tubules

Cystinuria

Aromatic odor

normal

Foul, ammonia-like odor

bacterial decomposition, urinary tract infection

Fruity, sweet

ketones (diabetes mellitus, salvation, vomitting) k - DSV

Maple syrup

Maple syrup urine disease

Mousy

Phenylketonuria

Rancid

tyrosinemia

Sweaty feet

Isovaleric acidemia

Cabbage

Methionine malabsorption

Bleach

Contamination

The group that is free is called

Carboxyl group

● Covalently linked polymers of amino acids

PROTEINS

Give me the primary structure of proteins

A. primary structure B. Secondary structure C. tertiary structure D. Quarternary structure

The different amino acids that compose a specific protein in a linear wa

Primary structure

The peptide chains are folded regularly which forms

Secondary structure - alpha helix and beta pleated sheets

Folded secondary structure into a 3D form ○ Considered a polypeptide

Tertiary structure

Combined tertiary polypeptide structure with other polypeptide

Quaternary Structure

The mRNA is partnered with an anti-codon with the help of the ribosomal complex

Translation

○ Purely made up of amino acids

Simple

Contain peptide chains on hydrolysis yield only amino acids

simple

Not entirely made up of amino acids only

conjugated

Comprise a protein (apoprotein) and a nonprotein moiety (prosthetic group)

conjugated

Conjugated sample

Lipids (lipoprotein), CHO (glycoprotein), porphyrins (hemoglobin), metals (ceruloplasmin)

Simple sample

albumin

Classification of Proteins (Function) (9)

enzymes hormones transport protein Immunoglobulins (Antibodies) Structural proteins Storage proteins energy source Osmotic force Blood coagulation

Catalyze chemical reactions

Enzymes

Control action of specific cells or organs

Hormones

Move substance inside the body

transport proteins

○ Gives protection against foreign objects

Immunoglobulins (antibodies)

○ Components of cells and tissues

● Structural proteins

○ Acts as reserves

● Storage proteins

Capable of affecting the distribution of water in the body

osmotic force

Clotting factors - fibrinogen

Blood coagulation

FIVE FRACTIONS OF PLASMA PROTEINS

Albumin, A1 globulins, A2 Globulins , B globulins, Y globulins,

α1-fetoprotein ○ α-antitrypsin ○ HDL

A 1 globulin

haptoglobin ○ ceruloplasmin ○ α2-macroglobulin

A2 globulin

○ transferrin ○ C-reactive protein

B globulin

Immunoglobulins

Y globulin

● Also known as transthyretin

PREALBUMIN

● Migrates ahead of albumin

pre-albumin

Transport protein of thyroid hormones T 3 and T4

Triiodothyronine and thyroxine - pre albumin

Binds with retinol-binding protein to form a complex that transports retinol (vitamin A)

PREALBUMIN

● Rich in tryptophan

pre-albumin

Hepatic damage

Decrease prealbumin

Acute phase inflammatory response

Decrease prealbumin

Tissue necrosis

● Decrease prealbumin

Sensitive marker of poor protein nutritional status

Decrease prealbumin

● Present in highest concentration

ALBUMIN

Increase in prealbumin

Steroids, alcoholism and chronic renal failure SAC

Albumin in the body can maintain the appropriate fluid balance in our body ■ Regulating colloid osmotic pressure of the intravascular fluid

○ Colloid osmotic pressure

○ Transcapillary escape rate

Rate of movement of albumin leaving the blood circulation

Can bind to thyroid hormones ■ Similar to pre albumin

bind to othersubstance

Can bind to conjugated bilirubin, iron, calcium and magnesium

ALBUMIN

Resulting in the inability of hepatocytes to synthesize albumin

hypoalbuminemia - liver disease

Inflammation and intestinal mucosal disease. ○ The interstitial fluid that contains albumin leaks out in the intestine and will be easily excreted esp. The person is suffering from diarrhea

Hypoalbuminemia - gastrointestinal loss

Kidney can't function properly and cannot filter all proteins → proteins will go out from the blood circulation→ urine

Loss in the urine in renal disease.

Seen in dehydration

hyperalbuminemia

● Absence of albumin

analbuminemia

Bakante ang albumin (lower left)

anaalbuminemia

Unusual molecular characteristics

Bisalbuminemia

Genetic in origin resulting from an autosomal recessive trait

bisalbuminemia

● condition of having two types of serum albumin that differ in mobility during electrophoresis

Bisalbuminemia

Consists of alpha1, alpha2, beta, and gamma fractions in electrophoresis

Globulins

● Acute-phase reactant

ALPHA 1 - ANTITRYPSIN

Neutralize trypsin-like enzyme that can cause hydrolytic damage to structural protein

ALPHA 1 - ANTITRYPSIN

Alpha 1 antitrypsin increase

Increased: inflammation, pregnancy, contraceptive use

Alpha 1 antotrypsin decrease

Deficiency: Severe, degenerative, emphysematous pulmonary disease

Synthesized initially by the fetal yolk sac and then by the parenchymal cells of the live

ALPHA 1 - FETOPROTEIN (AFP)

13 weeks’ gestation

Peak:

34 week’s gestation

Recede

Incomplete closure of embryonic neural tube

Spina bifida and neural tube defects

Incomplete spinal cord

Spina bifida and neural tube defects

Narrowing or absence of a portion of the intestine of the fetus

○ Atresia of the gastrointestinal tract

Not well; excessively fatigue

○ Fetal distress

Immunodeficiency disorder

○ Ataxia-telangiectasia

Increased level of tyrosine

tyrosinosis

Anti-D of the mother attacks the RBC with the D antigen of the fetus

Hemolytic disease of the newborn (HDN)

Hepatolenticular degeneration ■ Autosomal recessive inherited disease

○ Wilson’s disease

Kinky hair disease ■ There is a problem in the absorption of copper. Ceruloplasmin is not only a carrier of copper it also contains copper. If the body has a problem in the level of copper, then definitely the ceruloplasmin will be directly affecte

menke's syndrome / kinyky's hair disease