amino acids and classification of proteins Flashcards by genrev nicavera

Amino acids with non-polar R group

Have hydrocarbons as side chains.

Glycine (Gly)
Alanine (Ala)
Tryptophan (Trp)
Isoleucine (Ile)
Valine (Val)
Leucine (Leu)
Proline (Pro)
Phenylalanine (Phe)
Methionine (Met)

G A T I Val Leu Pro Phe Met

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Have hydrocarbons as side chains.

Amino acids with non-polar R group.

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Protein molecules with large amounts of this amino acids are
insoluble and non-reactive.

Example: Structural protein (Collagen)

Amino acids with non-polar R group

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Slices DNA and produces different
amino acids.
* One of the three most important
glucogenic amino acids.

It is used as a sweetener or flavor
enhancer.

aids in enhancing
stomach absorption, is present in some
medication formulations

glycine (GLY)

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H2N dash C dash C upper slant OH lower slant O

above the C is H

under the C is H

glycine

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It is used to treat conditions like benign
prostatic hyperplasia, schizophrenia,
stroke, and a few other uncommon
inherited metabolic problems.

glycine (GLY)

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In analgesics, antacids, antiperspirants,
cosmetics, toiletries, etc., this serves as
a buffering agent

glycine (GLY)

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It serves as an intermediary in the
production of several chemical
products and is also utilized in the
production of the herbicide glyphosate

Glycine (GLY)

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The primary amino acid in sugar
metabolism.
* Boosts immune system by
producing antibodies.

it is a source of energy for
muscles and the central nervous
system.

It is used to break down
tryptophan and vitamin B-6

A. Tryptophan
B. Leucine
C. Alanine

alanine (ALA)

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NH2 dash C dash COOH

above the C is H
below the C is CH3

alanine

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Essential for muscle growth and
regeneration and is involved in
energy production.

A. Leucine
B. Valine
C. Arginine

valine (VAL)

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has two CH3 and 1 CH as amino group

Valine (val)

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Used by the body to make proteins like
collagen.
* Critical component of cartilage, aids in
joint health, tendons and ligaments.

Lowers elevated blood sugar
levels and increases growth
hormone production.

Keeps heart muscle strong

proline (PRO)

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house like drawing structure

proline

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Helps with production of pigment
melanin.

Body can convert it into
tyrosine, which it then uses to
synthesize the neurotransmitters
dopamine and norepinephrine.

Used in some artificial sweeteners. It
tends to decrease appetite.

A. Glycine
B. Phenylalanine
C glutamine

phenylalanine (Phe)

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has a hexagon drawing shit followed by CH2 in amino group side

phenylalanine (Phe)

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An antioxidant. Helps in
breakdown of fats and aids in
reducing muscle degeneration

used in the treatment
of kidney stones, maintaining
healthy skin and also used in
controlling invade of pathogenic
bacteria.

methionine (Met)

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has H3C—–S——CH2——CH2 in amino group side

methionine (Met)

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Involved in the production of
vitamin B3 and serotonin
hormones.

tryptophan (Trp)

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This serotonin hormone plays a
vital role in maintaining our
appetite, regulating sleep and
boosting our moods

tryptophan (Trp)

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has a gord of gaara drawing as a amino group side

tryptophan (Trp)

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Involved in promoting protein
synthesis and growth hormones.

A. Isoleucine
B. Leucine
C. Lysine

leucine (Leu)

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has a CH3 —-CH——CH2 as amino group side

and CH3 above the CH.

leucine (Leu)

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Produce partial charges but do not receive or donate electrons.
* Increases solubility of proteins and enables hydrogen bonding
between polypeptide chains.

Amino acids with polar R group

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Amino acids with polar R group

serine (Ser) asparagine (Asn) glutamine (Gln) tyrosine (Tyr) cysteine (Cys) threonine (Thr) Threo, glu, cys, tyr, aspa, ser.

Maintains blood sugar levels, and boosts immune system A. Serine B. Valine C. Histidine

serine (Ser)

Myelin sheaths contain this amino acid.

serine (Ser)

has CH2OH

serine (Ser)

Mainly involved in the transportation of nitrogen into our body cells,

asparagine (Asn)

Formations of purines and pyrimidine for the synthesis of DNA, the development of the nervous system.

asparagine (Asn)

Improving our body stamina. A. Arginine B. Isoleucine C. Asparagine

asparagine (Asn)

has a H2N-----C-------CH2 as amino group. and O above the C

asparagine (Asn)

Promotes a healthy brain function and is necessary for the synthesis of nucleic acids – DNA and RNA. A. Glutamine B. Threonine C. Asparagine

glutamine (Gln)

Essential for helping to maintain normal and steady blood sugar levels A. Valine B. Glutamine C. isoleucine

glutamine (Gln)

Helps muscle strength and endurance. Gastrointestinal function, provides energy to small intestines

glutamine (Gln)

has a H2N-----C-------CH2--------CH2 as amino group. and O above the C

glutamine (Gln)

Plays a vital role in the production of the thyroid hormones -T3 and T4,.

tyrosine (Tyr)

Synthesizing a class of neurotransmitters (dopamine, norepinephrine and adrenaline) and melanin, which are natural pigments found in our eyes, hair, and skin.

tyrosine (Tyr)

Has HO-----hexagon drawing shit----followed by CH2 as amino group side.

tyrosine (Tyr)

Acts as an antioxidant. Protective against radiation, pollution and ultraviolet light. Detoxifier, necessary for growth and repair of skin A. Lysine B. Cysteine C. Glutamine

cysteine (Cys)

* It is important for making collagen. It affects the texture and elasticity of the skin. Provides resistance to our body.

cysteine (Cys)

has SH---CH2 as a amino group.

cysteine (Cys)

Helps in promoting the functions of the immune system A. Threonine B. Asparagine C. Glycine

threonine (Thr)

Aids in antibodies' production. * Required for formation of collagen. A. Asparagine B. threonine C. Cysteine

B. threonine

* Helps prevent fatty deposits in liver.

threonine (Thr)

Amino acids that is Negatively charged * Hydrophilic – soluble in water

Amino acids with acidic R group

asparatic acid (Asp) glutamic acid (Glu)

Plays a major role in metabolism * Promotes the synthesis of other amino acids. A. Arginine B. Tyrosine C. Aspartic acid

asparatic acid (Asp)

Increases stamina and helps protect the liver; DNA and RNA metabolism, immune system function. A. Asparagine B aspartic acid C. Threonine

asparatic acid (Asp)

Acts as a neurotransmitter. Mainly involved in the development and functioning of the human brain.

glutamic acid (Glu)

has OH---C-----CH2 as amino group side. has O above the C

asparatic acid (Asp)

has OH-----C-----CH2----CH2 as amino group side has an O above the C.

glutamic acid (Glu)

amino acid that is Positively charged * Hydrophilic – soluble in water

Amino acids with basic R group

lysine (Lys) arginine (Arg) histidine (His) "His Arg Lys"

Necessary for promoting the formation of antibodies, hormones, and enzymes and in the development and fixation of calcium in bones

lysine (Lys)

It is also a precursor for L-carnitine, which is essential for healthy nervous system function

lysine (Lys)

has CH2-----CH2----CH2-----CH3---NH3+ as a side chain.

lysine (Lys)

Helps in promoting the synthesis of proteins and hormones, A. Asparagine B. glutamine C. Arginine

arginine (Arg)

Detoxification in the kidneys, healing wounds, and maintaining a healthy immune system. A. Arginine B. Asparagine C. Tryptophan

arginine (Arg)

has H2N--C--NH--CH2--CH2--CH2 as a amino group. and NH above the C

arginine (Arg)

Involved in many enzymatic processes A. valine B. Tyrosine C. Histidine

histidine (His)

Involved in the synthesizing of both red blood cells (erythrocytes) and white blood cells (leukocytes).

histidine (His)

has a pentagon drawing shit with N above and HN below followed by CH2 as a amino group.

histidine (His)

Amino acids that must be supplied in the diet

Essential Amino Acids

help the body function and regulate neurotransmitters, chemicals in the brain that control mood and behavior.

Essential Amino Acids

Phenylalanine Valine Threonine Tryptophan Isoleucine Methionine Histidine Arginine (*but only essential during nitrogen balance) Leucine Lysine

Produce histamine. Maintain the myelin sheath.

histidine

Muscle metabolism in muscle tissue, immune function, hemoglobin production and energy regulation A. Leucine B. arginine C. Isoleucine

isoleucine

Protein synthesis, muscle repair, regulate blood sugar levels, stimulates wound healing and produces growth hormones. A. Leucine B. Histidine C. Tyrosine

leucine

Protein synthesis, hormone and enzyme production and the absorption of calcium, energy production, immune function, the production of collagen and elastin

lysine

Metabolism and detoxification, tissue growth and absorption of zinc and selenium, minerals. A. Glutamine B. Lysine C. Methionine

methionine

Precursor for tyrosine, dopamine, epinephrine and norepinephrine, structure and function of proteins and enzymes and the production of other amino acids. A. Phenylalanine B. Tyrosine C Tryptophan

phenylalanine

Structural proteins such as collagen and elastin, fat metabolism and immune function A. Histidine B. Glutamine C. Threonine

threonine

Maintain proper nitrogen balance and is a precursor to serotonin.

tryptophan

Stimulate muscle growth and regeneration and is involved in energy production. A. Valine B. Cysteine C. Lysine

valine

can be synthesized by adults but not by growing children, hence these are considered as semi-essential amino acids.

Semi-Essential Amino Acids

arginine histidine

Releasing hormones, cell division, wound healing, functioning of the immune system, removal of ammonia from the body. A. Arginine B. Asparagine C. Tyrosine

arginine

Produce histamine. Maintain the myelin sheath.

histidine

Amino acids that can be synthesized by the body.

Non- Essential Amino Acids

Alanine, asparagine glutamic acid glutamine cysteine aspartic acid glycine tyrosine proline serine mnemonics Almost, All, Girls, Go, Crazy, After, Getting, Taken, Prom, Shopping

Levels of Protein Organization

1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure

Linear arrangement of amino acids present in the polypeptide chain.

Primary Structure

The sequence of amino acids in a protein, is like the order of letters in a long word.

Primary Structure

determined by inherited genetic information.

Primary Structure

Primary Protein Structure Example

Dystrophin

Dystrophin Mutation

Duchenne Muscular Dystrophy Becker Muscular Dystrophy

Found in most proteins, consists of coils (a helix) and folds (b pleated sheet) in the polypeptide chain

Secondary Structure

refers to highly regular local sub-structures.

Secondary Structure

Secondary Structure Example

Antibodies/T cell receptor Hexokinase

determined by interactions among various side chains (R groups)

Tertiary Structure

Three-dimensional structure of a single protein molecule.

Tertiary Structure

Tertiary Structure Example

Myoglobin

Results when a protein consists of multiple polypeptide chains

Quaternary Structure

Connectivity between two (or) more polypeptide chain.

Quaternary Structure

These chains may be identical (or) different in primary structure.

Quaternary Structure

Quaternary Protein Structure Example

Hemoglobin

Hierarchical nature of protein structure

(Amino acid sequence) to （α-helix, β-sheet）to （Three-dimensional structure formed by assembly of secondary structures）to （Structure formed by more than one polypeptide chains）

sequence of a chain of amino acid

primary protein structure

local folding of polypeptide chain into helices or sheets

secondary protein structure

three dimensional folding pattern of a protein due to side chain interactions

tertiary protein structure

protein consisting of more than one amino acid chain

quaternary protein structure

Classification of Proteins According to Structure:

a. Fibrous Proteins b. Globular Proteins

Classification of Proteins According to Composition:

a. Simple Proteins b. Conjugated Proteins

Proteins involved in formation of body structures of animals. * Have secondary structures. * Stable structure * Insoluble in water

Fibrous Proteins

Structural functions * Polypeptide chains form long strands. * Ex: Collagen, myosin, fibrin, keratin

Fibrous Proteins

Have tertiary structures and some may have quaternary structures.

Globular Proteins

Polypeptide chains are tightly coiled and folded to form a sphere.

Globular Proteins

Relatively unstable structures * Soluble in water

Globular Proteins

Metabolic functions * Ex: All enzymes, antibodies, insulin, hemoglobin, globulin, hormones

Globular Proteins

Pure proteins that do not contain any other substance. * Ex: fibrous proteins, globular proteins

Simple Proteins

Made up of two portions attached together; a protein portion attached to a non-protein known as the prosthetic group.

Conjugate Proteins

Further classified into many groups based on the properties of the different prosthetic groups:

Conjugate Proteins

Conjugated Proteins

Lipoprotein -----Prosthetic group *Lipid Glycoprotein-----Prosthetic group *Polysaccharide Chromoprotein-----Prosthetic group *Pigment molecule Metalloprotein---Prosthetic group *Metal ion Nucleoprotein---Prosthetic group *Nucleic acid

Where can you find Lipoprotein

Component of cell membrane

Where can you find Glycoprotein

Cells and blood serum

Where can you find Chromoprotein

Hemoglobin, myoglobin

Where can you find Metalloprotein

Hemoglobin, myoglobin, cytochromes

Where can you find Nucleoprotein

Chromosomes and ribosomes

amino acids and classification of proteins Flashcards

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