Week 5 Flashcards
proteins
- associated with strength and muscle
- important for wound healing
- structural and functional role in cells
what does excess meat result in?
high saturated fat intakes
what is protein found in?
- milk
- eggs
- legumes
- many whole grains
FRUIT=NO PROTEIN
proteins as working molecules (functional)
- enzymes
- antibodies
- transport vehicles
- hormones
- cellular “pumps”
- oxygen carriers
proteins for structure
- tendons
- ligaments
- scars
- fibres of muscles
- cores of bone and teeth
- filaments of hair
- material of nails
protein components
- made of carbons, hydrogen and oxygen
- contain nitrogen (only one)
- some amino acids also contain sulphur
- composed of amino acids
- 20 different aa make up most of the proteins of living tissue
amino acids
- an amine group at one end-nitrogen containing part
- acid group at the other
- a distinctive side chain (side group) attached to the carbon at that centre of the backbone
***gives identity and chemical nature to each amino acid
side chains (side groups) of aa
what makes the aa different from each other
1. size
2. shape
3. electrical charge
- large strands of aa = large protein molecules
essential amino acids (indispensable)
- aa that cannot be synthesized at all by the body or cannot be synthesized in sufficient amounts
- can only be replenished from foods
- body NEEDs these aa to perform work
- body can make other aa from fragments derived from carbs or fat to form backbones and nitrogen from other sources
nonessential amino acids (dispensable)
- aa that can be synthesized by the body
- the body can make these aa from
- fragments derived from carbs or fat to form backbones
- nitrogen from other sources
indispensable/essential aa
- an aa that is normally nonessential
- in circumstances when the need exceeds the body’s ability to produce it, it must be supplied by the diet
recycling amino acids
body makes some aa but also breaks down proteins to reuse those aa
when do we reuse amino acids?
food proteins (after digestion) and body proteins (after cellular work) are dismantled freeing their aa
- this provides body a tiny aa pool (150g)
- provides raw materials to build protein molecules it needs
protein turnover
bringing in and breaking down proteins
- about 300 to 400 g/day
amino acids used for energy if requires
- tissues can break down their own proteins in times of fuel or glucose deprivation
- working proteins are sacrificed
- most dispensable proteins used first (ex. small proteins of blood and muscle)
- structural proteins are guarded until their used is forced by dire need (ex. proteins of heart)
peptide bond
- connects one aa to another
- formed between the amine of one aa and the acid group of the next aa
- CONDENSATION reaction - forms a chain of aa with side chains bristling out from backbone
condensation reaction
joins amine of one aa and acid group of next aa
primary structure of peptide bonds
amino acid sequences
secondary structure of peptide bonds
polypeptide shapes
1. determined by weak electrical attractions within chain
2. positively charges hydrogens attracts nearby negatively charged O2
3. sections of chain may twist into helix or fold into a pleated sheet giving proteins strength and stability
tertiary structure of peptide bonds
polypeptide tangles
1. long polypeptide chains twist and fold into variety of complex tangles shapes
2. side groups may attract or repel each other (hydrophilic or phobic)
3. disulfide bridges determine tertiary structure
4. shape gives characteristics
hydrophilic side groups
on the surface of water
- “water loving”
hydrophobic side groups
are hidden in the middle
- “water fearing”
quaternary structures of peptide bonds
multiple polypeptide interactions
1. interactions between 2 or more polypeptides
2. some polypeptides work together in large complexes (
2. some protein strands function alone while other proteins are composed of several strands
variety of proteins
proteins perform different tasks dictated by shape
1. globular proteins are water soluble (proteins of blood)
2. some proteins form hollow balls (carry are store material in interior)
3. some proteins are much longer than wide (proteins of tendons)
collagen
a protein from which connective tissues are made
- tendons, ligaments, scars and foundations of bones and teeth
- acts like glue between cells
insulin
helps regulate blood sugar
enzymes
protein catalysts
- all enzymes=proteins
catalyst
substance that facilitates a chemical reaction without itself being altered in the process
inherited amino acid sequences
for each protein there exists a standard aa sequence
- sequence is specified by heredity
- wrong aa can be disastrous to health
sickle-cell disease
- inherited variation in aa sequence - abnormal hemoglobin
- one aa in a critical position has been replaced by a different one
genetic expression and the nutrients
- every human cell nucleus contains DNA for making every protein
- cells monitor nutrient concentrations in fluids surrounding them and triggers a cascade of molecular events leading to expression or suppression of certain genes
denaturation
the irreversible change in a protein’s shape
- caused by heat, acids, bases and alcohols
what is denaturation important for?
digestion of food protein
- stomach acids open-up a proteins structure
- allows digestive enzymes to make contact with the peptide bond and cleave them
denaturing proteins due to cooking
a protein that binds both biotin and iron is denatured, liberating them for digestion
- without cooking some things you will be biotin and iron deficient
ex. changes that occur to egg white when an egg is cooked
digestion of proteins
- certain acid-tolerant proteins, digest proteins from food that have been denatured by acid
- coating of mucus secreted by stomach wall protects its proteins from attack by either acids or enzymes
what is the normal acid of the stomach?
PH about 2
- no food is acidic enough to make it stronger
digestion of proteins in the mouth
protein is crushed by chewing and is moistened with saliva
digestion of protein in the stomach
- acid helps to uncoil the protein’s tangled strands so that the stomach’s protein-digesting enzyme (pepsin) can attach the peptide bonds
- lining is protected from acid and enzymes by a mucus coating secreted by stomach cells
pepsin
the stomachs protein-digesting enzyme
- works best in an acidic environment
- breaks down protein chains in the stomach
- cleaves aa strands into polypeptides and a few aa
digestion of proteins in the SI
receives small denatured pieces of protein from stomach
- most are polypeptides, but a few are single aa
***where most protein digestion occurs
alkaline juices
released from the pancreas
- neutralize the acid delivered by the stomach
- pH increased to about 7 (neutral)
proteases
protein-digesting enzymes from the pancreas and SI continue to break down protein until nearly all that is left are dipeptides, tripeptides or single aa
what pH do enzymes work best in?
neutral pH (7)
single amino acid supplements
may compete for absorption sites or overwhelm a carrier resulting in possible deficiency in another aa
cells along the SI
absorb single aa
1. have enzymes on their surfaces that split most tripeptides and dipeptides into single aa, which are then absorbed
2. some di- and tripeptides are absorbed into cells where they are split into single aa before being released into bloodstream
larger peptide molecules
a few larger peptide molecules can escape the digestive process altogether and enter the bloodstream intact
- this may give information about external environment
- may stimulate an immune response and have a potential role in food allergies
amino acids in the bloodstream
- carried to liver
- used by liver or released into blood to be taken up by other cells
amino acids in the liver
used in…
1. protein synthesis
2. synthesize a nonessential aa and released into bloodstream for cells
amino acids in the cells
used for…
1. make proteins for their own use
2. make proteins that are released into lymph of blood for other uses
3. when neccessary, body cells use aa for energy
roles of proteins in the body
- supporting growth and maintenance
- building enzymes, hormones and other compounds
- maintaining fluid and electrolyte balance
- maintaining acid-base balance
- clotting of blood
- providing energy and glucose
proteins supporting growth and maintenance
- build proteins of new tissue (embryo, scar tissue, new hair and nails, etc.)
- protein helps replace worn-out cell structures
- red blood cells live only 3-4 months
- cells lining intestinal tract live only 3 days
- skin cells are constantly being shed and replaced
hormones
chemical messengers secreted by a number of body organs in response to conditions that require regulation
- each has a specific organ or tissue and elicits a specific response
- some are made from aa (proteins)
tyrosine
component of both epinephrine and norepinephrine, and is used to make both melanin and throxine
tryptophan
starting material for serotonin and niacin
antibodies
produced by the immune system
- large proteins of the blood
proteins maintaining fluid and electrolyte balance
- too much fluid in a cell = cell ruptures
- too little fluid in a cell = cell is unable to function
- cells retain fluid needed by maintaining internal proteins
- fluid is kept within blood vessels by proteins that are too large to freely move across capillary walls
water in cell vs protein
water can diffuse freely into and out of cells
- protein cannot diffuse freely, and proteins attract water
large proteins and fluid
the large proteins attract and hold water within the vessels, preventing water from freely flowing into spaces between cells
maintaining acid-base balance
proteins are important to maintain this balance
acids
compounds that release hydrogens
bases
compounds that accept hydrogens
what acts as buffers to maintain blood pH?
blood proteins
- protein buffers pick up hydrogens when there are too many in the bloodstream
- they release hydrogens when there are too few in the bloodstream
acidosis
- condition of excess acid in the blood
- below-normal pH
alkalosis
- condition of excess base in the blood
- above-normal pH
acidosis and alkalosis
can cause coma or death
- proteins can be denatured, disrupting many body processes
clotting of blood
special proteins provide the netting on which blood clots are built