proteins semi finals

proteins

ØLarge molecules of unbranched polymers of amino acids

ØAre found in every cell in the body

ØAre involved in most of the body's functions and life processes

monosaccharides

what is the basic unit of carbohydrates

glycosidic bond

what connects monosacc to another monosacc

fatty acid

what is the basic unit of lipids

Esther Bond

what connects one fatty acid to another

amino acid

what is the basic unit of protein

peptide bonds

what connects one amino acid to another

it has nitrogen

what makes your protein unique

16%

protein has how many % nitrogen content?

dietary protein to mouth

Protein digestion and absorption starting point

mouth

this part of the Protein digestion and absorption has no enzyme present to solubilize/digest the protein

stomach

Protein digestion and absorption 2nd station

HCl

this maintains the acidity of the stomach at approximately 2-3ph

HCl

this denatures protein in the stomach

pepsin

this enzyme hydrolyzes peptide bonds in the stomach

stomach

initial digestion of proteins occur in?

small intestines

main digestion in proteins occur in?

large polypeptides

after protein is hydrolyzed in the stomach, it becomes?

small intestine

large polypeptides then goes to where?

trypsin

chymotrypsin

carboxypeptidase

aminopeptidase

small intestines enzymes

epithelial cells

where are the 4 enzymes of the small intestines located?

amino acids

after the large polypeptides is acted upon the 4 enzymes, what does it form or become?

intestinal lining

amino acid from small intestine then goes inside the?

active transport

the amino acid is delivered to the bloodstream in the intestinal lining via ?

proteins

all proteins are enzymes but not all enzymes are

biocatalyst

this function of proteins speeds up the rate of chemical reaction

by lowering/shortening the activation energy (shortcut, less hago)

the biocatalyst speeds up te chemical reaction by?

activation energy

energy needed to achieve for the chemical reaction to take place

transport system

this function of proteins works in bilirubin metabolism

bilirubin

because of this, jaundice exist

liver

in bilirubin metabolism, unconjugated bilirubin needs to be transported going to the ?

albumin

what carries the unconjugated bilirubin going to the liver?

albumin

majority of the protein in our body is?

maintenance of oncotic pressure

this Function of proteins

oncotic and hydrostatic

two types of pressure

oncotic pressure (force going inwards)

this type of pressure keeps the blood/tissue fluid inside the blood vessel

albumin

main actor that maintains/strengthens the oncotic pressure

hydrostatic pressure (force outwards)

pressure that keeps the blood away from the blood vessel

hydrostatic

if the albumin is low, what pressure is abundant/mas mo kusog?

edema

more abundant hydrostatic pressure which is caused by low albumin results to?

maintain the fluid

oncotic and hydrostatic should be balance to?

blood coagulation

this Functions of protein involves clotting of the blood

platelets

what makes the mesh (kugang)

amino acid

is an organic compound that contains both an amino (-NH2) group and a carboxyl (-COOH) group.

all amino acids

what contains amino group (NH2) and a carboxyl group (acid group)

side chain

what makes an amino acid different to another amino acid?

•(1) nonpolar amino acids

(2) polar neutral amino acids

(3) polar acidic amino acids

(4) polar basic amino acids.

categories of amino acids

nonpolar amino acids

this category of amino acid cannot be dissolved in water.

NONPOLAR AMINO ACID

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

POLAR NEUTRAL AMINO ACID

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

POLAR ACIDIC AMINO ACIDS

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

POLAR BASIC AMINO ACIDS

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

essential amino acid (9)

this type of amino acid must be consumed in diet, gikan sa kinaon

nonessential amino acid (11)

this type of amino acid must be from the body, can be synthesized in the body

conditionally essential

this type of amino acid cannot be synthesized due to illness or lack of necessary precursors

arginine

•Premature infants lack sufficient enzymes needed to create ?

50 / fewer

how many amino acids does peptides have

greater than 50

how many amino acids does protein have

condensation

peptide bonds link to amino acid through?

primary structure

this is a linear level of protein structure

secondary and tertiary levels of structure

this is a helix/helical level of protein structure

quaternary structure

this is a 3D level of protein structure

denaturing

Alteration of the protein's shape and thus functions

heat

acids

bases

salts

mechanical agitation

causes of alteration of protein structures

primary structure

what is the only structure protein that is unchanged by denaturing

plasma

blood treated with anticoagulants to prevent clot formation then centrifuged to remove the cells

serum

blood that is allowed to form a fibrin clot then

centrifuged to remove the cells and the clot

lavender

hematology top tube, BB

electrophoretic mobility

migration of proteins based on size and charges