PROTEINS PT.2 Flashcards by Tolentino, Marielle L.

Specialized proteins involved in defending the body from antigens.

One way ____________ counteract antigens is by immobilizing them so they can be destroyed by white blood cells.

ANTI - BODIES

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are responsible for muscle contraction and movement.

Examples of these proteins include actin and myosin.
As myosin and actin interact in the presence of ATP, they form a tight compact.

CONTRACTILE PROTEIN

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Are proteins that facilitate biochemical reactions.

They are often referred to as catalysts, because they speed up chemical reactions.

ENZYMES

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myosin and actin interact in the presence

ATP

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CHARACTERISTICS OF PROTEINS

Can be broken down into separate units by the use of enzyme.
Consist of amino group and acid group (ampotheric).

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Are messenger proteins which help to coordinate certain bodily activities.

HORMONAL PROTEINS

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examples of hormonal proteins

INSULIN, OXYTOCIN, SOMATOTROPHIN

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FUNCTIONS OF PROTEINS

 Antibodies
 Contractile proteins
 Enzymes
 Hormonal proteins
 Structural proteins
 Storage proteins
 Transport proteins

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regulates glucose metabolism by controlling the blood-sugar concentration.

INSULIN

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stimulates contractions during childbirth.

OXYTOCIN

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Are fibrous and stringy and
because of this formation, they provide support for
various body parts.

STRUCTURAL PROTEINS

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is a growth hormone that stimulates protein
production in muscle cells.

SOMATOTROPHIN

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EXAMPLE OF STRUCTURAL PROTEINS

KERATIN, COLLAGEN, ELASTIN

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strengthen protective coverings such as skin, hair, quills, feathers, horns, and beaks.

KERATIN

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provide support for connective tissues such as tendons and ligaments.

COLLAGEN & ELASTIN

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basic structural building blocks of protein.

 molecules having one amino group , one carboxyl group, one H atom and one specific
group (R group) attached to the central C atom.

AMINO ACIDS

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store amino acids for the body to use later.

STORAGE PROTEIN

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another protein that stores iron in the transport protein, hemoglobin.

FERRITIN

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which move molecules from one place to another around the body.

CARRIER PROTEINS

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is one of these and is responsible for transporting oxygen through the blood via red blood cells.

HEMOGLOBIN

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proteins are “_________”

UNIQUE

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Contains C, H, O, N

 Has both hydrophobic & hydrophylic ends.

 Makes polypeptide then makes proteins

 Differ in R-group

 R-group can be acidic, basic or neutral

AMINO ACIDS MONOMER

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are another that operate in the electron transport chain as electron carrier proteins.

CYTOCHROMES

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EXAMPLES OF PROTEIN RICH FOOD

Lean white meats
Soy
Beef
Beans
Eggs
Dairy
Seafood

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NON - POLAR AMINO ACID

Glycine, Alanine, Valine, Leucine, Isoleucine, Proline, Phenylalanine, Methionine, Tryptophan

POLAR NEUTRAL AMINO ACID

Serine, Cysteine, Threonine, Asparagine, Glutamine, Tyrosine

POLAR ACIDIC AMINO ACID

Asparatic acid and Glutamic acid

POLAR BASIC AMINO ACID

Histidine, Lysine and Arginine

an amino acid that contains one amino group,one carboxyl group,and nonpolar side chain. * When incorporated into a protein,such amino acids are hydrophobic(water-fearing).

NON - POLAR AMINO ACID

an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral (neither acidic nor basic).

POLAR NEUTRAL AMINO ACID

R-group can be ____, _____, OR ________

ACIDIC, BASIC, NEUTRAL

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

POLAR ACIDIC AMINO ACID

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

POLAR BASIC AMINO ACID

* Have straight side chains. * (threonine, glycine, serine, alanine)

ALIPHATIC AA's

Those that contain additional acidic or basic group classified into:

A. Aliphatic AAs B. Aromatic or cyclic AAs.

* Contain a ring structure * (tryptophan, phenylalanine, tyrosine)

AROMATIC OR CYCLIC AA's

* those with additional amino acid group. * (Lysine, Arginine, Histidine)

BASIC AA's

Those that contain additional carboxyl group.  (aspartic acid, glutamic acid)

ACIDIC AA's

are AAs having aliphatic side- chains with a branch ( a carbon atom bound to more than two other carbon atoms.)

Branched- chain amino acids (BCAA)

There are _____________ used by the ribosomes to make proteins.

20 common α-amino acids

are used clinically to aid in the recovery of burn patients, and supplementation of strength athletes.

BRANCHED - CHAIN AMINO ACIDS (BCAA)

EXAMPLES OF BCAA

(leucine, isoleucine, valine)

CLASSIFICATIONS OF AMINO ACID

 According to the structure of side chain.  According to polarity of the side chain (R group)  According to the nutritional requirements  According to the metabolic fate

Glutamate from ____________.

wheat gluten

Greek word of Tyrosine from cheese

"TYROS"

cannot be synthesized itself by the organism (usually referring to humans), and therefore must be supplied in the diet.

ESSENTIAL AMINO ACID

help the body function andregulate neurotransmitters, chemicals in the brainthat control mood and behavior.

ESSENTIAL AMINO ACID

are generally compact, soluble, and more/less spherical to oblate or egg-shaped.

GLOBULAR PROTEINS

ALBUMIN IN ____

EGG

CASEIN IN _______ & ______

MILK AND CHEESE

are typically elongated and insoluble. Long coiled or folded chains of amino acids bound together in parallel line.

FIBROUS PROTEINS

GLOBULIN IN ______

RED BLOOD CELLS

hey are able to provide support for cells and tissues

FIBROUS PROTEINS

can be synthesized by adults but not by growingchildren, hence these are considered as semiessential amino acids.

SEMI - ESSENTIAL AMINO ACID

EXAMPLE OF ESSENTIAL PROTEIN

* Tryptophan * Valine * Threonine * Isoleucine * Leucine * Lysine * Phenylalanine * Methionine

* These can be synthesized by the body to meet the biological needs. * need not to be consumed through the diet.

NON - ESSENTIAL AMINO ACID

refers to highly regular local sub-structures. * Extended conformation of polypeptide chains

SECONDARY STRUCTURE

* Linear arrangement of amino acids present in the polypeptide chain. * Each protein has a distinctive number and sequence of amino acid residues

PRIMARY STRUCTURE

HEMOGLOBIN

QUARTERNARY STRUCTURE

refers to three dimensional structure of a single protein molecule. Connectivity between two (or) more polypeptide chain. * These chains may be identical (or) different in primary structure.

TERTIARY STRUCTURE