Amino acids and Proteins Flashcards by max eriksen

what is the most abundant macro-nutrient in the body?

PROTEIN

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what are the functions of proteins in the body?

signaling
structure
immunity
transport
enzymes
fluid balance
buffers

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what is the chemical messenger made in 1 part of the body regulates another part?

hormones

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what is the hormone made of multiple amino acids?

peptide hormones

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thyroid hormones (thyroxine) and catecholamines are derived from which amino acids?

Tyrosine

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tyrosine gives rise to what Amino Acid Derivatives?

thyroid hormones (thyroxine)
catecholamines

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what are catecholamines?

Neurotransmitters in brain

dopamine
epinephrine
norepinephrine

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Histidine gives rise to what Amino Acid derivatives?

Histamine

immune repsonse, associated with allergies

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what is histamine’s functions?

immune response, associated with allergies

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tryptophan gives rise to what Amino Acid derivatives?

Serotonin, Niacin, and melatonin

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what are the functions of serotonin?

Neurotransmitter regulating mood, sleep, and appetite

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what are the functions of melatonin?

regulates sleep-wake cycle

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what are the small protiens that act as regulators of growth and differentiation?

Cytokines

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Interleukin-1 (IL-1), Tumor Necrosis Factor (TNF-Alpha), Interleukin-6 (IL-6), Interleukin-10 (IL-10), and C-Reactive Proteins (CRP) are examples of what?

Cytokines

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what are some examples of cytokines?

Interleukin-1
Interleukin-6
Interleukin-10
Tumor Necrosis Factor
C-Reactive Proteins

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when are cytokines produced?

they are produced during acute and chronic inflammation, cancer, obesity, stress, injury and degenerative disc disease

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what is the Cytokine that is the best indicator of Inflammation?

C-Reactive Protein

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what is the Cytokine that breaks down adipose tissue?

Interleukin-6

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when is the Cytokine interleukin-10 produced?

produced during exercise

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what is the Function of the Cytokine C-Reactive Protein?

it is the best indicator of inflammation

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what is the Cytokine that is produced during exercise?

Interleukin-10

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what is the function of Interleukin-6?

it breaks down adipose tissue

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Some of the biological functions of proteins are structural. what are the two structural proteins?

Fibrous Proteins

Contractile Proteins

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Collagen, elastin, and keratin are examples of what structural proteins?

Fibrous proteins

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Actin and myosin are examples of what structural proteins?

Contractile Proteins (65% of muscle composition)

what are examples of fibrous proteins?

collagen elastin keratin

what are the examples of contractile proteins?

actin | myosin

Immunoglobulins and antibodies are examples of what biologically functional proteins?

Immunoproteins

what are the general examples of immunoproteins?

immunoglobulins, and antibodies

the Y-shaped proteins containing 4 proteins that binds to antigens and inactivate?

Immunoproteins

what are the five classes of immunoproteins?

``` IgG IgA IgM IE IgD ```

the class of immunoproteins that is found in 75% of plasma?

IgG

The Class of immunoprotein that is in secretions such as (tears,saliva, and breast milk)?

IgA

The class of immunoprotein that was originally malaria and is a response to all antigens?

IgM

The class of immunoprotein that is for Allergies?

IgE

The class of immunoprotein for chronic infections?

IgD

The characteristics of IgG?

found in 75% of plasma

The characteristics of IgA?

found in secretions such as (tears, saliva, and breast milk)

The characteristics Of IgM?

originally malaria, and a response to all antigens

The characteristics of IgE?

the response to Allergies

The characteristics of IgD?

released during Chronic infections

the type of protein that has the biological function to combine with other susbstances and acts as a mode of transport through body?

Transport Proteins

what is the biological function of transport proteins?

to combine with other substances and acts as a mode of transport through the body

what are some examples of transport proteins?

Albumin Hemoglobin Transferrin Vitamin D

Albumin, Hemoglobin, Transferrin, and Vitamin D are examples of what Biologically functional proteins?

Transport Proteins

Albumin is the Transport protein for what?

Calcium, Zinc, Vitamin B6

Hemoglobin is the transport protein for?

Oxygen

Transferrin is the transport protein for?

Iron

Vitamin D is the Transport Protein for?

Binding protein-Vitamin D

The type of protein that has the biological functions to be a biological catalyst, regulate metabolic pathways, limit rates, and is necessary for life?

ENZYMES!

what are the biological functions of enzymes?

Biological catalyst Regulate Metabolic Pathways limit rates of reactions necessary for life

what are characteristics of Biological catalysts?

- they speed up reaction by lowering activation energy needed for reaction to occur. - they are not used up during this process

Fluid Balance is an example of what?

a biological function of protein

Some ways that proteins regulate fluid balance?

- water interacts with several groups on proteins - charged residues, peptide backbone, hydroxyl groups - water attracted to protein

some ways that a protein deficiency would affect the fluid balance biological function?

-Protein deficiency can cause fluid to leak into interstitial spaces causing Edema

what is Kwashiorkor?

a protein Malnutrition

what are some causes of a protein deficiency that would affect fluid balance?

- Deficiency can be caused by kidney disease, large wounds, liver disease, and Malnutrition - Kwashiorkor- Protein Malnutrition

a biological function of proteins is to buffer? what is a buffer?

a compound that prevents a change in pH

Proteins act as buffers in?

plasma

Hemoglobin is a buffer in?

red blood cells

what is the buffer in red blood cells?

hemoglobin

What is the buffer in Plasma?

Proteins

what is a compound that prevents a change in pH?

Buffer

a protein Deficiency that can be caused by kidney disease, large wounds, liver disease, and Malnutrition would affect what biological function of proteins?

fluid balance

-water interacting with several groups on proteins -charged residues, peptide backbone, hydroxyl groups -water attracted to protein are some of the ways that proteins perform what biological function?

Fluid Balance

buffers work when pH is?

pH is low (too many H+) | pH is High (too few H+)

When a base is added, what happens to the [H+]?

Decreases

when a base is added, which part of the protein donates a H+?

amino group

how many essential amino acids are there?

9 essential | must get from our diet (exogenous)

how many amino acids are non-essential?

11 non-essential | Body can make (endogenous)

what does exogenous mean?

-must get from outside body. | from our diet

what does endogenous mean?

-from inside our body | body can make

Amino acids are the building block of?

proteins

which isomer of an amino acid is corn spelled clockwise?

L-amino acids

which isomer of an amino acid is corn spelled counter clockwise?

D- amino acids

what percentage of amino acids found in the liver are used to make new proteins and N-containing compounds?

20%

20% of amino acids found in the liver are used to make?

new proteins and N-containing compounds

what are the new proteins made in the liver?

enzymes (remain in liver) Plasma proteins acute phase proteins (inflammatory response)

what amino acids are used by the muscles?

Branched chain amino acids only | Valine, Leucine, and Isoleucine

albumin, prealbumin, alpha-1 proteins, alpha-2 proteins, beta-globulins, Y-globulins are what type of proteins?

plasma proteins

what are the plasma proteins?

``` albumin prealbumin alpha-1 globulin alpha-2 globulin beta-globulin Y-globulin ```

what is the most abundant plasma protein, and maintains osmotic pressure. its a transport protein that is used to measure protein status?

albumin

characteristics of the plasma protein albumin?

- most abundant plasma protein - maintains osmotic pressure - transport nutrients - measure of protein status, but slow to change (2 weeks) - deficiency will cause Kwashiorkor

what nutrients does albumin transport?

``` vitamin B6 zinc calcium copper smaller fatty acids tryptophan ```

vitamin B6, zinc, copper, calcium, smaller fatty acids, and tryptophan are transported by what plasma protein?

albumin

a deficiency of which two plasma proteins would cause kwashiorkor?

albumin | prealbumin

what is a transport protein, that is a measure of protein status with a half-life of 2 days?

prealbumin

which plasma protein is a glycoprotein, high density lipoprotein?

alpha-1 globulins

which plasma protein contains glycoprotein, haptoglobin, ceruloplasmin, prothrombin, and very low density lipoproteins?

alpha-2 globulins

which plasma protein contains transferrin, and low density lipoproteins?

beta-globulins

which plasma protein contains immunoglobulins?

Y-globulins

what is the definition of non polar?

hates water (hydrophobic)

the non-polar amino acids?

``` Glycine alanine Valine Leucine Isoleucine Methionine Proline Phenylalanine tryptophan ```

Glycine is what type of amino acid?

Non-Polar, and Aliphatic

what is the definition of polar?

loves water (hydrophilic)

serine is what type of amino acid?

Polar

Alanine is what type of amino acid?

Non-Polar, and Aliphatic

Theronine is what type of amino acid?

Polar

Cysteine is what type of amino acid?

Polar

Valine is what type of amino acid?

Non-Polar, and Aliphatic

Leucine is what type of amino acid?

Non-Polar, and Aliphatic

Isoleucine is what type of amino acid?

Non-Polar, and Aliphatic

Tyrosine is what type of amino acid?

Polar, and Aromatic

Asparagine is what type of amino acid?

Polar

Glutamine is what type of amino acid?

Polar

Methionine is what type of amino acid?

Non-Polar, and Aliphatic

Proline is what type of amino acid?

Non-Polar, and Aliphatic

Phenylalanine is what type of amino acid?

Non-Polar, and Aromatic

Aspartate is what type of amino acid?

Polar, and Acidic

Tryptophan is what type of amino acid?

Non-Polar, and Aromatic

Glutamate is what type of amino acid?

Polar, and Acidic

Lysine is what type of amino acid?

Polar, and Basic

Arginine is what type of amino acid?

Polar, and Basic

Histidine is what type of amino acid?

Polar, and Basic

what is the definition of an Aliphatic amino acid?

contains a hydrocarbon chain in the R group

what type of amino acid contains a hydrocarbon chin in the R group?

Aliphatic

what is the definition of an Aromatic amino acid?

contains a 6 membered ring in the R group

what type of amino acid has a 6 membered ring in the R group?

Aromatic

what is the definition of an acidic Compound?

(negatively charged) | contains a carboxylic acid in the R group

when an acid is added, which part of the protein accepts the H+?

carboxylic group

what type of amino acid contains a carboxylic acid in the R group?

Acidic

what type of amino acid contains an N in the R group?

Basic (positively charged)

what is the definition of a Basic amino acid?

contains an N on the R group

The characteristics of Glycine?

``` Non-Polar (Aliphatic) uncharged Only Amino Acid without a Chiral C Found in high concentrations in collagen allows bends in peptide nonessential ```

``` Non-Polar (Aliphatic) uncharged Only Amino Acid without a Chiral C Found in high concentrations in collagen allows bends in peptide nonessential which amino acid is this? ```

Glycine

the characteristics of Alanine?

Non-Polar (Aliphatic) uncharged | Released from muscle during starvation, exercise, or after a high carbohydrate meal to be turned into glucose

Non-Polar (Aliphatic) uncharged Released from muscle during starvation, exercise, or after a high carbohydrate meal to be turned into glucose. which amino acid is this?

Alanine

what are the characteristics of Valine?

Non-Polar (Aliphatic) uncharged Branched Chain Amino acid Essential

Non-Polar (Aliphatic) uncharged Branched Chain Amino acid Essential which amino acid is this?

Valine

what is the disease when Valine replaces glutamate in hemoglobin and causes red blood cells to fold incorrectly?

sickle cell anemia | genetic mutation that occured over time to protect against malaria

what happens to cause sickle cell anemia?

Valine (nonpolar) replaces Glutamate (polar) in hemoglobin. | -causes red blood cells to fold incorrectly

the characteristics of Leucine?

Nonpolar (Aliphatic), uncharged amino acid Branched chain amino acid essential high concentration in globulin and albumin(hemoglobin) partial degradation yields HMG Coa (precursor to cholesterol)

-Nonpolar (Aliphatic), uncharged amino acid -Branched chain amino acid -essential -high concentration in globulin and albumin(hemoglobin) -partial degradation yields HMG Coa (precursor to cholesterol) which amino acid is this?

Leucine

what are the characteristics of Isoleucine?

Non-Polar (Aliphatic), uncharged AA Branched Chain AA Essential Structural isomer of Leucine

``` Non-Polar (Aliphatic), uncharged AA Branched Chain AA Essential Structural isomer of Leucine which amino acid is this? ```

Isoleucine

the disease when there is a genetic deficiency of enzymes required to metabolize branched chain amino acids?

Maple Syrup Urine Disease | Urine with color, odor, and viscosity of maple syrup

the characteristics of maple syrup urine disease?

- genetic deficiency of enzymes required to metabolize branched chain amino acids.(valine, leucine, Isoleucine) - Symptoms: urine with color, odor, and viscosity of maple syrup - if untreated can cause brain damage and health - treatment: avoid high protein food for life

what are the characteristics of Methionine?

``` Nonpolar (Aliphatic) uncharged essential S-containing Precursor for: -S-adenosyl methionine (SAMe) -Cysteine ```

``` Nonpolar (Aliphatic) uncharged essential S-containing Precursor for: -S-adenosyl methionine (SAMe) -Cysteine which amino acid is this? ```

Methionine

the function of SAMe in the body?

methylates compounds

SAMe is required by the body to make?

``` Carnitine creatine epinephrine melatonin glutathione taurine myelin basic protein ```

SAMe may be used to treat?

osteoarthritis, depression

Populations who should not use SAMe?

those with bipolar disorder patients on antidepressants cancer patients

what are the characteristics of Proline?

- nonpolar, uncharged amino acid - Not aromatic - nonessential - disrupts alpha-helix and beta pleated sheet structure. - found in high concentrations in collagen

-nonpolar, uncharged amino acid -Not aromatic -nonessential -disrupts alpha-helix and beta pleated sheet structure. -found in high concentrations in collagen which amino acid is this?

proline

what are the characteristics of phenylalanine?

nonpolar (aromatic), uncharged AA essential precursor for tyrosine

nonpolar (aromatic), uncharged AA essential precursor for tyrosine which amino acid is this?

phenylalanine

what is the genetic disorder that lacks enzyme necessary to metabolize phenylalanine?

phenylketonuria

what are the characteristics of Phenylketonuria?

- genetic disorder that lacks enzyme necessary to metabolize phenylalanine - causes brain damage - 1/10,000 babies born with - Phenylalanine found in Nutrasweet and anything with protein - Treatment: avoid Phenylalanine in diet (low protein)

what is the genetic disorder where you are missing 1 phenylalanine in protein that regulates transport of chloride ions across cell membranes?

Cystic Fibrosis | most common genetic disorder

the characteristics of Cystic Fibrosis?

- genetic disorder affecting 1/2,000 humans - missing 1 phenylalanine in protein that regulates transport of chloride ions across a cell membrane - does not fold correctly, protein is degraded - causes mucus to build up (lung and digestion issues)

what are the characteristics of Tryptophan?

``` nonpolar (aromatic) uncharged AA essential precursor for: -serotonin -melatonin -Niacin ```

``` nonpolar (aromatic) uncharged AA essential precursor for: -serotonin -melatonin -Niacin which amino acid is this? ```

Tryptophan

the neurotransmitter needed for mood, behavior, Body T, and appetite?

serotonin

the hormone needed for biological clock and acts as an antioxidant?

Melatonin

what are the characteristics of Serine?

polar, uncharged AA - nonessential - important in active site of enzymes - able to H-Bond - Hydroxyl group is Phosphorylated for protein regulation

``` polar, uncharged AA -nonessential -important in active site of enzymes -able to H-Bond -Hydroxyl group is Phosphorylated for protein regulation which amino acid is this? ```

Serine

what are the characteristics of Threonine?

Polar, uncharged AA - essential - also a site of phosphorylation in protein regulation

Polar, uncharged AA -essential -also a site of phosphorylation in protein regulation which amino acid is this?

threonine

what are the characteristics of Cysteine?

Polar, uncharged AA - nonessential - thiol (SH) group is a proton donor in GLUTATHIONE - antioxidant properties - important in proteins that participate in REDOX - important for cross-linking proteins through disulfide bonds

Polar, uncharged AA -nonessential -thiol (SH) group is a proton donor in GLUTATHIONE -antioxidant properties -important in proteins that participate in REDOX -important for cross-linking proteins through disulfide bonds which amino acid is this?

Cysteine

Albumin and insulin are 2 of many proteins stabilized by?

(Cystine) disulfide bridges

what are the characteristics of Tyrosine?

``` Polar, uncharged AA -nonessential -precursor for: thyroid hormones (thyroxine) Melanin (pigment) -Catecholamines dopamine norepinephrine epinephrine ```

the catecholamine that relates to mood, behavior, and cognition?

Dopamine

Dopamine is a catecholamine that controls what?

mood, behavior, cognition

what is the catecholamine that is a derivative of tyrosine and is a stress hormone?

Norepinephrine

Norepinephrine is what type of hormone?

stress hormone

what is the catecholamine responsible for fight or flight?

Epinephrine

Epinephrine is responsible for what?

fight or flight

what are the characteristics of Asparagine?

Polar, uncharged Amino Acid - found at the beginning an d end of alpha-helix because of H-bonding in R-Group - forms acrylamide with sugar at high temperature.

Polar, uncharged Amino Acid -found at the beginning an d end of alpha-helix because of H-bonding in R-Group -forms acrylamide with sugar at high temperature. what is this amino acid?

Asparagine

HCL denatures what protein structures?

2, 3 , and 4 structures of proteins

is the globular class of protein shape polar or non-polar?

polar

the shape of this protein is decided by secondary, tertiary, and quaternary?

globular