Chapter 6 Proteins and Amino Acids

proteins

H,O,C, and N arranged as strands of amino acids

amino acids

the building blocks of proteins
amino acids differ in their side chains

how many amino acids

20
9 essential

amino acid side chains

differ in size, shape, and electrical charge

components of an amino acid

central carbon, amine group, acid group, and side chain

essential amino acids

can't be synthesized by the body or not enough is produced to meet physiological needs
without the essential nutrients, the body cannot make the proteins it needs to do its work

recycling amino acids

food proteins after digestion and body proteins after they are finished their cellular work are broken down for their component amino acids
these amino acids are raw materials for cells to build protein molecules

uses of recycled amino acids

used for energy, nitrogen discarded as waste, recycles something valuable while reducing the burden of disposing of nitrogen, can be an emergency fund in times of low fuel, glucose, or protein

peptide bond

bond that connects different amino acids, forming a link in a protein chain

essential amino acids

histidine
isoleucine
leucine
lysine
methionine
phenylalanine
threonine
tryptophan
valine

protein folding and coiling

caused by side chains attracting and repulsion from each other
the coil folds and flips over itself to take a functional shape
the different shapes allow proteins to perform different tasks

primary structure

the amino acid sequence
this determines the shape and shape determines function

secondary structure

coiling
alpha helixes and beta pleated sheets

tertiary structure

folding
formed by alpha helixes and beta sheets around each other

quaternary structure

arrangement of a multiple folded protein
ex: hemoglobin

sickle cell anemia

hemoglobin is abormal; mix-up with the sixth amino acid and it alters the proteins to be unable to carry and release oxygen
cells collapse into crescent shapes
can cause abnormal blood clotting, strokes, bouts of severe pain, susceptibility to infection,

gene expression

the nucleus contains DNA to product every human proteins but some genes are expressed and some are not;
some cells specialize in making certain proteins

denaturation

irreversible change in a protein's folded shape brought about by heat, acids, bases, alcohol, salts of heavy metals, etc.
ex: HCl in the stomach or cooking an egg

where does protein digestion begin

in the stomach

role of HCl

breaks down proteins in stomach and activates pepsin
uncoil the protein to allow pepsin to attack the peptide bonds

stomach lining

protected against attack by acid and enzymes by a coat of mucus secreted by its cells

digestion in small intestine

most proteins have been denatured into smaller pieces
alkaline juice from the pancreas neutralizes the acid; this allows the enzymes to complete the final breakdown of the protein strands

pepsin

enzyme in stomach that breaks down proteins into short polypeptides and amino acids to be taken to the small intestine

pancreatic enzymes

complete the digestion of proteins into di- and tripeptides and amino acids

brush border enzymes

enzymes within the intestinal lining that split the di- and tripeptides

amino acids after digestion of proteins

absorbed as single amino acids and released into the blood stream
carried to the liver to be used or released into the blood to be take up by other cells in the body
cells can link the amino acids together to make proteins to keep for their own or to go i

central dogma

DNA-->mRNA-->proteins

requirement for protein synthesis

ALL ESSENTIAL AMINO ACIDS must be present

sequence of a protein determined by:

genes

transcription

messenger RNA copies the genetic information from DNA
takes place in the nucleus

translation

genetic information in RNA is converted into the amino acids sequence of a protein
mRNA takes it outside of the nucleus for translation to occur
tRNA collects amino acids from the cell fluid and brings them to the mRNA

protein turnover

continuous breakdown and synthesis of body proteins involving the recycling of amino acids

majority of body's proteins found in

muscle tissue; allow the body to move and can release amino acids for energy if needed
affects shape and strength of bones, teeth, skin, tendons, cartilage, blood vessels, etc.

acid-base balance

proteins help maintain the acid-base balance of various body fluids by acting as buffers

antibodies

proteins form the immune system moelcules that fight diseases

blood clotting

proteins provide the netting on which blood clots are built

energy and glucose

proteins provide some fuel for the body's energy needs

enzymes

proteins facilitate needed chemical reactions

fluid and electrolyte balance

proteins help to maintain the water and mineral composition of various body fluids

gene expression

proteins associate and interact with DNA, regulating gene expression

hormones

proteins regulate body processes; some are proteins or are made from amino acids

transportation

proteins help transport needed substances (lipids, minerals, and oxygen) around the body

energy density of proteins

4 kcal/gram

amino acids to glucose

amino acids can be converted to glucose, fatty acids never can
amino acids therefore can maintain a blood glucose level
the nitrogen from the amine groups are stripped and incorporated into the liver as urea and excreted through the urine

three uses for oversupplied amino acids

amine groups discarded
residues can either meet immediate energy needs, make glucose for storage as glycogen, make fat for energy storage

storage of proteins

no storage center for proteins, excess must excrete the amine group and use the residues
therefore, during starvation proteins are taken from small proteins in the blood, then from tissues in muscles, liver, or other organs

four conditions for wasting amino acids

when body lacks energy from other sources
when diet supplies more protein than the body needs
when body has too much of a single amino acid (ex: from a supplement)
when diet supplies protein of low quality with too few essential amino acids

DRI intake for proteins

0.8 grams for each kilogram of body weight
1.8 grams/kilogram
1 kilogram=2.2 pounds
minimum amount is 10% of total calories and no higher than 35%
women: 46 grams per day men: 56 grams per day

nitrogen balance

amount of nitrogen consumed compared with the amount excreted in a given time period
this is the goal for healthy, non-pregnant adults (consume enough to replace what is used every day)

positive and negative nitrogen balance

more protein at the end of the day than they had at the beginning ex: growing children, pregnant women
losing more nitrogen than they are taking in ex: illness or injury triggers this, amino acids and energy are needed to fuel body's defenses and fight th

nitrogen equilibrium

intake and outtake of nitrogen are equivalent
this is desired

complete protein

supplies all essential amino acids
body must have all essential amino acids to build proteins; if one is missing the amino acids will be excreted

incomplete protein

low in 1 or more essential amino acid

complementary proteins

2 or more incomplete proteins; amino acid assortments complement each other in a way that essential amino acids missing from one are supplied by the other
must be eaten in the same day
ex: grains and legumes, seeds/nuts,and vegetables

excess proteins

create too much ammonia (NH3) and that stresses the kidneys
too much NH3=toxic
excess proteins=extra calories=extra fat

harms to a high protein diet

o Low in plant foods (fiber, vitamins, phytochemicals)
o Increase risk for heart disease
o Linked with colon cancer
o Stresses kidneys
o Increases bone loss
o Recommendation: no more than 2x RDA for protein

protein-energy malnutrition

world's most widespread malnutrition problem; includes both marasmus and kwashiorkor
prevalent in Africa, Central America, South America, Middle East, and East and South Asia
strikes early in childhood

marasmus

form of PEM related to protein malnutrition and infections with recognizable symptoms like edema
occurs most commonly in children from 6-18 months on a diet of low energy and low protein quality

top contributors of protein in the US

beef, poultry, milk

effects of marasmus

wasting and weakening of muscles, stunted brain development, slow metabolism, no fat under skin to insulate against cold, stunted growth, skin loses elasticity and moisture, digestive tract lining deteriorates and absorption fails, anemia, low immunity be

kwashiorkor

disease resulting from extremely low protein intake
symptoms resemble marasmus but without wasting of body fat
proteins and hormones to maintain fluid balance are gone and fluid leaks out of the blood and accumulates in the belly and legs causing edema
of

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