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unit frickin d
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sensor
detects change
effector
returns whatever back to its previous state
control center
activates effector
6 essential nutrients
proteins, carbs, lipids, nucleic acids, vitamins, and minerals
monomers
the subunits of all nutrients
what is the fundemental component for all macromolecules
Carbon (is in all of the essential nutrients and macromolecules)
dehydration synthesis
the removal of a water molecule which assembles a macromolecule
requires enzymes
hydrolysis
the addition of a water molecule which disassembles a macromolecule into its subunits
requires enzymes
Carbs
main source of energy for the body
Carbon + hydrogen + oxygen
(CHO) usually in a 1:2:1 ratio
monosaccharides + the 3 forms
simple sugars consisting of 3-7 carbon atoms.
Glucose, fructose, galactose.
They have the same chemical formula of C6H12O6, but are in different arrangement (isomers)
dissacharides + the 3 forms
simple carbohydrates consisting of 2 monosaccharides
maltose - glucose + glucose
sucrose - glucose + fructose
lactose - glucose + galactose
polysaccharises + the 3 forms
complex carbohydrates formed by many monosaccharides in one.
Different forms of polysaccharides:
cellulose - structural material for plants
starch - storage form of carbohydrates in plants
glycogen - storage form of carbohydrates in animals
lipids
form cell membranes, energy storage, protection of internal organs, insulation
C + H + O
insoluble in water
what are lipids made of
glycerol bonded to fatty acids
monoglycerides - glycerol + 1 fatty acid
diglycerides - glycerol + 2 fatty acids
triglycerides - glycerol + 3 fatty acids
saturated vs unsaturated lipids
saturated - contain only single bonds between carbon atoms
unsaturated - contain double bonds between carbon atoms
one monounsaturated, or more polyunsaturated
saturated fats are found in…
animals
unsaturated fats are found in…
plants
also could help with lowering blood cholesterol
what are proteins
C + H + O + N
(carbon, hydrogen, oxygen, and nitrogen)
functions of protein is blood clotting, structure and support, muscle action, and transport
what are proteins made of
they are chains of amino acids joined by peptide bonds.
what are amino acids made of
(C+H) + amino group + acid group + “R” group
C+H = carbon and hydrogen separate
amino group = part with nitrogen and hydrogen
acid group = part with oxygen and carbon and hydgrogen
“R” group = variable of the protein. This is what makes different proteins
all add up to C+H+O+N
how many amino acids are there
because of the R group, there are 20 different types of amino acids. the body can synthesize 11, and we need to consume 9 of them, which are called essential amino acids.
peptide
several amino acids bonded together
polypeptide
chain of peptides
proteins are determined by:
one or more polypeptides folded into a unique shape that determines its properties and functions
what are nucleic acids
make up the chemical code that directs growth and development
(C+H+O+N+P)
DNA and RNA
DNA (deoxyribonucleic acid) - codes for production of proteins
RNA (ribonucleic acid) - helps assemble proteins
what are nucleic acids composed of
long chains of nucleotides
nucleotides
composed of:
5C sugar + nitrogen base + phosphate group
5C sugar = CHO (carbohydrate simple sugars) with 5 carbons
nitrogen base = rungs on the DNA ladder
phosphate group = backbones (spiral structure/ladder sides)
4 types of nucleotides
adenine
cytosine
thymine
guanine
one amino acid is made up of
3 nucleotides
vitamins
organic (contain carbon and hydrogen) compounds that serve as coenzymes (help enzymes out), and help with tissue devellopment and disease resistance
minerals
inorganic compounds that are essential for hemoglobin, hormones, enzymes, and vitamins
what are enzymes
protein molecules that speed up chemical reactions
how do enzymes work
by lowering the activation energy of the reaction.
enzymes have a specific shape, and can bind to the reactions it needs to bind to.
Substrate binds to the active site (shape) which changes the reactants, making it more likely to form new bonds
factors that effect enzyme action
temperature
pH
competitive inhibitors
non-competitive inhibitors
temperature effecting enzymes
temperatures outside of an enzyme’s optimal range will result in denaturing
denature
when an enzyme is out of its optimal range (the settings at which the enzyme works the best), it denatures and loses its shape, losing its function
enzymes are not…
consumes or chemically changed. They can be used over and over
pH
pH outside of an enzyme’s optimal range denatures the enzyme
competitve inhibitors
molecules that attatch to the active site of the enzyme, preventing subrate from binding to the active site
non-competitive inhibitors
changes the shape of the enzyme by attatching to a regulatory site, which changes the active site
accessory organs in the digestive system
liver, pancreas, gallbladder, and salivary glands
sphincter between small intestine and large intestine
ileocecal sphincter
sphincter between esophagus and stomach
esophageal sphincter
sphincter between stomach and small intestine
pyloric sphincter
ingestion
taking in food
digestion
chemically and mechanically breaking down food particles into smaller particles
mechanical digestion
breaking food into smaller pieces to INCREASE SURFACE AREA
chemical digestion
use of enzymes to breakdown macromolecules into their subunits
absorption
passing nutrients from digestive tract into circulatory system (blood stream)
egestion
eliminating undigested food and waste into feces.
passage of food from mouth to butt
mouth → pharynx → esophagus → stomach → small intestine → large intestine → rectum → anus
carbohydrates primary job
energy and structural support
protein primary job
build cells, do work inside organisms, and act as catalysts (enzymes), blood clotting, muscle action
lipids primary job
long term energy storage, forming cell membranes (phospholipid), protecting internal organs (fat production), and forming hormones