Proteins Flashcards by Gay Amor Tipolo Gacang

Q

is an amino acid in which the amino group, the carboxyl group and the hydrogen atom are attached to the a-carbon atom

A

a-amino acid

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Q

All amino acids are alpha-amino acids except _____ which is an imino acid.

A

Proline

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Q

is an amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain.

A

Nonpolar amino acid

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Q

is an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral.

A

Polar neutral

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Q

is an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain

A

Polar basic

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Q

is an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain

A

Polar acidic

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Q

CLASSIFICATION OF AMINO ACIDS:

G,A,V,L,I,P,F,M,W

A

Nonpolar amino acid

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Q

CLASSIFICATION OF AMINO ACIDS:

S,C,N,T,Q,Y

A

Polar neutral

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Q

CLASSIFICATION OF AMINO ACIDS:

H,K,R

A

Polar basic

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Q

CLASSIFICATION OF AMINO ACIDS:

D,E

A

Polar acidic

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Q

CLASSIFICATION OF AMINO ACIDS:

D,E

A

Polar acidic

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Q

a standard amino acid needed for protein synthesis that must be obtained from dietary sources because the human body cannot synthesize it in adequate amount.

A

ESSENTIAL AMINO ACIDS

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Q

Synthesized by the body.

A

NON-ESSENTIAL AMINO ACIDS

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Q

ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:

R*,H,M,I,L,K,W,T,F,V

A

ESSENTIAL AMINO ACIDS

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Q

ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:

C,A,N,D,E,Y,S, Q,G,P

A

NON-ESSENTIAL AMINO ACIDS

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Q

is a protein that contains all of the essential amino acids in the same relative amounts in which the body needs them. This may or may not contain all of the nonessential amino acids

A

COMPLETE DIETARY PROTEIN

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Q

is a protein that does not contain adequate amounts, relative to the body’s needs, of one or more of the essential amino acids

A

INCOMPLETE DIETARY PROTEIN

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Q

is an essential amino acid that is missing, or present in inadequate amounts, in an incomplete dietary protein

A

LIMITING AMINO ACID

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Q

are two or more incomplete dietary proteins that, when combined, provide an adequate amount of all essential amino acids relative to the body’s needs. Ex. Rice and beans servings.

A

COMPLEMENTARY DIETARY PROTEINS

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Q

Necessary for the synthesis of neurotransmitter serotonin (5-hydroxytryptamine). A natural relaxant, helps alleviate insomnia by inducing normal sleep; reduces anxiety and depression

A

Tryptophan

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Q

Can be metabolized to niacin Vit. B3 if needed

A

Tryptophan

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Q

Used to synthesized melatonin (5-methoxy-N-acetyltryptamine)

A

Tryptophan

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Q

Precursor of dopamine, norepinephrine, epinephrine
Promotes healthy thyroid functioning

A

Tyrosine

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Q

enhance energy, increase endurance, and aid in muscle tissue recovery and repair.

A

Valine, Isoleucine, Leucine

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lowers elevated blood sugar levels and increases growth hormone production

Valine, Isoleucine, Leucine

precursor for L-carathine which is essential for healthy nervous system function.

Lysine

for adequate absorption of calcium and bone development in children

Lysine

Is antioxidant. It helps in breakdown of fats and aids in reducing muscle degeneration. Helps lower cholesterol levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys

Methionine

principle supplier of sulfur, which inactivates free radicals. Is a natural chelating agent for heavy metals and helps detoxify the body of these metals

Methionine

Adequate ______ prevents disorders of the hair, skin and nails

Methionine

Beneficial for healthy nervous system. It may be useful against depression and suppressing appetite

Phenylalanine

Used to produce dopamine and norepinephrine, chemicals that promote alertness, elevate mood, decrease pain, aid in memory and learning, and reduce hunger and appetite

Phenylalanine

Type of Phenylalanine: natural form. May improve rigidity, walking disabilities, speech difficulties and depression associated with Parkinson’s disease

D-phenylalanine

Type of Phenylalanine: can be converted into L-tyrosine, which is in turn converted into L-DOPA. L-DOPA is a precursor for dopamine, norepinephrine (noradrenalin), and epinephrine (adrenaline)

L-phenylalanine

Removes toxic substances released from breakdown of muscle protein during intensive exercise

Alanine

antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants such as vitamin E and selenium.

Cysteine

Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.

Glutamine

Component of skin and is beneficial for wound healing. It acts as neurotransmitter

Glycine

Important for the synthesis of red and white blood cells.

Histidine

It is a precursor for histamine which is good for sexual arousal. Improve blood flow.

Histidine

It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.

Threonine

Enhances stamina, aids in removal of toxins and ammonia from the body, and beneficial in the synthesis of proteins involved in the immune system.

Aspartic Acid

plays role in intracellular signaling.

Proline

plays role in blood vessel relaxation, stimulating and maintaining erection in men, production of ejaculate, and removal of excess ammonia from the body.

Arginine

Is a molecule that has a positive charge on one atom and a negative charge on another atom, but which has no net charge.

Zwitterion

It is the pH at which an amino acid exists primarily in its zwitterion form.

Isoelectric Point

formed by a biochemical reaction that extracts a water(H2O) molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid.

Peptide Bonds

is a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid

Peptide Bonds

The linear sequence of amino acids within a protein is considered the _______ of the protein.

Primary Structure

Proteins are built from a set of only _____ amino acids

Twenty (20)

The largest group of amino acids have _______ side chains

Nonpolar

Hydrophobic side chains interact with each other via __________

weak van der Waals interactions.

TYPES OF PEPTIDE BOND: w/ 2 or more amino acids

Dipeptide

TYPES OF PEPTIDE BOND: w/ 3 or more amino acids joined together in a chain

Tripeptide

TYPES OF PEPTIDE BOND: w/ 10 or 20 amino acid residues are present in a chain

oligopeptide

TYPES OF PEPTIDE BOND: w/ longer unbranched chain of amino acids

Polypeptide

Uterus-Contracting Hormone (also stimulates lactation)

Oxytocin

Enhances reabsorption of free water and plays a role in Blood pressure control

Vasopression (ADH or antidiuretic hormone)

pain killers neuromodulators in the brain and spinal cord; involved with pain perception, movement, mood, behavior, and neuroendocrine regulation

Enkephalins

Found in most living cells as antioxidant & promote tissue growth

Glutathione

(governs release of thyrotropin) or TSH or thyroid-stimulating hormone

TRH (Thyrotropin Releasing Hormone)

Pressor Agent. Can increase blood pressure by vasoconstriction.; can also trigger thirst or the desire for salt. Is responsible for the release of the pituitary gland's ADH

Angiotensin II

Inhibits Growth Hormone Release (used to treat ulcers)

Somatostatin

Hypotensive Vasodilator (acts on smooth muscle)

Bradykinin

Potent Vasoconstrictor (structurally similar to some snake venoms)

Endothelin

Honey Bee Venom (used to treat rheumatism)

Mellitin

Hyperglycemic Factor (used as an anti-diabetic)

Glucagon

Pancreatic Hormone (used in treatment of diabetes)

Insulin

amino acid sequence — drives the folding and intramolecular bonding of the linear amino acid chain, which ultimately determines the protein's unique three-dimensional shape

primary structure

Hydrogen bonding between amino groups and carboxyl groups in neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known as alpha helices and beta sheets, these stable folding patterns make up the _____________ of a protein

secondary structure

The ensemble of formations and folds in a single linear chain of amino acids — sometimes called a polypeptide — constitutes the _______ of a protein.

tertiary structure

refers to those macromolecules with multiple polypeptide chains or subunits.

quaternary structure

It is the hydrogen bonding of the peptide hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern.

Secondary structure

It includes three-dimensional folding pattern or a protein due to side chain interactions

Tertiary structure

It is the protein consisting of more than one amino acid chain.

Quaternary Structure