Digestive system Flashcards
What are the 4 types of macromolecules
Proteins
Carbohydrates
Lipids
Nucleic Acids (DNA, RNA)
What is a marcomolecule?
a large complex organic molecule found in living organisms. They are essential and needed in large quantities (Macro)
What is dehydration synthesis?
an Anabolism process that removes water to form water molecules.
going from simple to complex
2H+0->H2O
what is Hydrolysis?
A catabolism process that breakers macromolecules by adding water
compels to simple
Catabolism
a process that releases energy
hydrolysis
Anabolism
a process that requires energy
dehydration synthesis
What are carbohydrates?
Main energy source for body
end in ose ( sucrose, Glucose)
what are the types of carbohydrates
monosaccharides- simple sugars (one ring)
Disaccharides - made by combining two monosaccharides (two rings)
Polysaccharides - complex carbohydrates (many rings together)
what are the lab test that could identify carbs
A Benedict‘s reagent test can identify simple sugars
A iodine reagent test can identify starches
what are lipids made of?
lipids are composed of one glycerol and three fatty acids forming a triglyceride?
What are the types of fats
saturated fats, have no double bonds contain all possible hydrogen, and a solid at room temperature think of coconut oil or bacon grease
unsaturated fats, have one or more double bonds between carbons liquid at room temperature think of olive oil bent configuration
trans fats
created through hydrogenation, adding hydrogen to unsaturated fats
increase in bad cholesterol and decrease in good cholesterol hydrogens are on opposite sides
which type of fats are bent in configuration?
Unsaturated fats
What type of fats have opposite hydrogen’s that are alternating?
Trans fats
what is a test that we can do to test for lipids?
Glazed/brown paper test
what are nucleic acids?
Types of chains of nucleoid that transfer and expressed genetic information
What are the two types of nucleic acids?
DNA which stores and transfers genetic information
RNA which builds proteins from amino acids
What are nucleic acids made of?
nucleotides consist of a phosphate group, a sugar, and a nitrogenous base
What are proteins?
their polymers made up of amino acids and contain carbon, hydrogen, oxygen nitrogen, and sometimes sulphur too
What is the primary function of proteins in the body?
Eden growth, maintenance blood clotting transport, structural function, primarily non-energy source
what are proteins made up of?
Composed of amino acids, which contain an amino group a carboxyL group and in R group
A-C
l
R
How many different types of amino acids are there?
20
The body cannot synthesize how many different types of amino acid that are essential? So where must they be attained from?
Nine so they must be attempted from our diet
How are protein made?
through dehydration synthesis, the removal of H2O, which is a catabolism process
what are amino acids linked by and what did they form?
Amino acids are linked by peptide bonds to form polypeptides
what is a peptide bond? And a polypeptide.
A link between amino acids
A polypeptide is a link between many peptide bonds
Protein structures
primary structure a connections of the letters, think of the letter in the alphabet
Secondary structure a twisting due to hydrogen bonding think of writing words
Tertiary structure more folding due to interactions between our groups think of sentences
Quantity structure large globe proteins made of polypeptides put together think of writing a paragraph
What does denaturation?
A change in protein shape due to changes in temperature or pH
If factor is removed, it possibly may return to a shape originally
When denatration occurs there’s a chance it may be permanent. What is that called?
coagulation
When a protein shape occurs through denaturation, it will lose its normal function and have no function
what would happen to approach if it were exposed to extreme heat or changes in pH?
It would be nature and probably end up in coagulation, resulting in permanent change and the function of the protein
describe the role of nucleic acids in the body
Storage of genetic information and transfer through DNA or helping build proteins from amino acids with RNA
compare and contrast dehydration, synthesis, and hydrolysis
Explain why trans fats are considered unhealthy
What type of test can we do to test for proteins?
biuret reagent test as it identifies peptide bonds
what are vitamins and minerals?
Essential nutrients needed in small amounts
what are vitamins?
Organic compounds that have carbon that act as coin enzymes and our primarily eating and tissue growth development and immunity
What are minerals
Inorganic compounds that help form hormones enzymes and haemoglobin important for bone and card structures
What are enzymes?
enzymes are protein molecules, that acts catalyst to increase reaction rates
Typically end in ase
Each enzyme has a specific shape and only combined to a particular substrate think of a lock and a key
Where do substrate bind to the enzyme?
At the active site
why do each enzyme have particular shapes and only combined to specific substrate
because they have particular functions and enzymes and substrates are like lock and keys, so they can only go with one and one
what are the optimal conditions for enzyme activity?
Optimal temperature 36°C
Optimal pH most enzymes work best at 6 to 8 pH but stomach enzymes work best at one to three pH and intestinal enzymes work best at eight pH
what are factors affecting enzyme activity?
Substrate concentration, temperature and pH
explain substrate, concentration and how it affects and activity
more concentration equals more collisions and enzyme activity increases until all active sites are occupied
explain how temperature affects enzyme activity
Higher temperature equals more collisions too much heat equals denaturation, making enzymes not functional
explain how pH affects and enzyme activity
Enzymes only work within a specific pH range too many hydrogen or hydroxide ions can change enzyme shape and function
what is an enzyme inhibitor?
Stop enzymes from binding to a substrate
What are the two different types of inhibitors?
Competitive inhibitor and non-competitive inhibitor
what is a competitive inhibitor?
It binds to the active site of a enzyme, blocking the substrate from attaching
what is a non-competitive inhibitor
The inhibitor binds away from the active site so it changes the enzymes 3-D shape making it useless
how do enzyme inhibitors affect the body?
Positive positively negatively and neutrally, depending on what and where the enzyme is being inhibited
when a protein is heated it loses all levels of organization besides its primary structure when this happens the protein is said to be
denatured
Proteins differ from fats and carbohydrates in that proteins
contain nitrogen
