Lipids ( Fats. phospholipids. steroid alcohols )
used to insulate the organic structure every bit good as protect variety meats
-better for you
-one or more dual bonds between Cs
-oils ( helianthus. flax )
-lower thaw point
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-worse for you
-single bonds between Cs
-higher runing points
-2 fatty acids. 1 glycerin. – phosphate group. + choline group -hydrophobic dress suits
Groups of phospholipids move together and make a protective membrane with the hydrophilic caputs one the exterior and really indoors of the cell and the hydrophobic tails confronting one another.
-4 hydrocarbon ironss fused together
-many functional groups attached
-a large portion of the cell membrane
– cells turn cholesterin into vitamin D and gall salts
Carbohydrates ( mono. di. poly carbohydrates )
Monosaccharides- clasp energy and shop it for cellular respiration Simple sugars – supply short term energy and storage
-most common one is Glucose ( C6H12O )
-glactose and fructose are chemical isomers intending they have the same chemical expression but different constructions.
2 monosaccharoses combined
glucose + glucose = malt sugar
Many monosaccharoses combined together to make STARCH. CELLULOSE and GLYCOGEN
Starch ( amylose-simpler diagram ) – long term energy and storage Glycogen ( more branched diagram ) – fresh glucose is turned into animal starch and stored for subsequently usage
Cellulose- works cells are made of this which is why they are stiff. Used in digestion in worlds. cleans out colon and bowels.
Proteins – constructing blocks of life
Amino acids – organic compound incorporating an amino and a carboxyl group Have R-groups or side ironss that are responsible for how it bonds with other aminic acids. The bonds between amino acids are peptide bonds. NON POLAR LIKES NON POLAR
POLAR LIKES POLAR
POSITIVE LIKES NEGATIVE
A clump of aminic acids bind together through a certain sequence coded in the DNA -the figure and order of acids is specific to each different protein
Peptide chains get down to bond with each other through the R groups. Bonds done in the secondary construction are normally done between amino acids near together. This causes the polypeptide concatenation to go ALPHA HELIX or a BETA PLEATED SHEET
-main bonds are hydrogen bonds between the carboxyl and O atoms
More bonds occur between aminic acids but this clip they are father apart from each other doing it to flex and turn up even more
DISULPHIDE BOND- a bond between cysteine amino acids
ELECTROSTATIC BOND- an ionic bond between negative a positive side ironss HYDROGEN BONDS- a bond between polar r-groups
HYDROPHOBIC INTERACTIONS- a bond between non-polar r-groups
Highest degree of organisation
The bonding of two or more third proteins. doing a batch of proteins into functional proteins.
Dehydration synthesis- remotion of water and seting two molecules together Hydrolasis- adding of H2O and interrupting apart two molecules Redox- give an negatron off = oxidized. acquiring an negatron = reduced
The changeless province cells try to be
Certain things base on balls in and out of the cell at specific times and rates so
that the internal environment corsets stable. Concentration gradient- difference between and are of high and an country of low concentration Brownian motion- the uninterrupted motion and hit between molecules in a liquid
Passive conveyance – needs no energy
Simple diffusion- the motion of molecules from an country of high to low concentration. Small uncharged molecules like O are passed through the membrane of a cell easy so that the cell can hold O.
Osmosis- motion of H2O across a semi permeable membrane from and country of higher concentration to an country of lower concentration
Facilitated diffusion- motion of molecules that are excessively large to be passed through the phospholipid bilayer or are non lipid soluble. Protiens throughout the membrane aid with the motion
Carrier protiens – move merely specific molecules. Adhere to that molecule and travel through a series of motions and form altering to travel the molecule into the cell and so goes through those stairss once more to return to its original form. Channel protiens- proteins with a hole in the center that allows bigger molecules to go through in and out of the cell.
Active transport- requires excess energy
Cells need higher concentrations of certain foods to last so sometimes molecules are moved against the concentration gradient utilizing applied energy. traveling them against the concentration gradient is active conveyance
Sodium K pump
Not many stuffs are excessively large to go through through the cell membrane. For those that cant. the cell membrane can wrap around the molecule to absorb it.
-when the cell wraps around the molecule to absorb it
-pinocytosis- cell “drinking” . little bead of extracellular fluid with little molecules within it ( most common ) -phagocytosis- cell “eating” . big bead of extracellular fluid with organic or bacterial molecules Exocytosis
-when the cyst moves to the exterior. The cyst fixes the cell membrane and the contents are moved out of the cell
Acts as a barrier for the cell. protecting the internal environment from the external environment. Cell membranes around the cell every bit good as around the cell organs. -regulates what goes in and out of the cells and cell organs
4 components= phospholipid bilayer. proteins. cholesterin and saccharides
2 fatty acids. 1 glycerin. – phosphate group. + choline group provides the physical barrier
separates the extracellular fluids from the intracellular fluids
-integral= edge in the hydrophobic inside of the cell
-peripheral=bound in the hydrophilic outside of the cell
-figments of the cytoskeleton= microtubules making a model for the membrane
act as piecing system and gives the cell fluidness
can link to proteins ( glycoproteins ) or lipoids ( glycolipids ) and act as
communicators between cells
Rush up reactions 1000000x
Reduce required reaction energy
Very sensitive to their environment
When exposed to extreme conditions they can “denature” and go wholly dysfunctional Aren’t created nor destroyed during a reaction
pH and temperature affect the activity of an enzyme because they will merely work at at that place maximal when in the perfect conditions. Anything other than that wont be optimum and finally do the enzyme to denature.
Enzymes are proteins with a depression called the active site. R groups stick out of the active side and pull substrates with similar R groups. The catalyzing occurs in the active site.
How is the active site form determined by the 4 degrees of protein construction? -polypeptide chain- sequence of aminic acids and how the R groups react with eachother which causes a form -then they fold and flex into secondary and third construction doing for the concluding form -the substrate is polar so the R groups confronting out into the active site have to hold some kind of mutual opposition to pull it.
SIMPLE ENZYMES- enzymes made merely of protein and the map consequences from the 3D agreement of the amino acids
CONJUGATED ENZYMES- enzymes with both protein and non protein parts a ) apoenzyme- protein portion of the enzyme
B ) cofactor-non protein portion. stopping point to active site.
WITHIN A COFACTOR
-coenzyme= vitamins that are altered during a reaction. These have to be replaced by unchanged molecules before a new substrate can attach -activators=minerals ( metal ions )
non merely do environmental factors ( pH and temperature ) consequence enzymes but substances can suppress the actions of an enzyme.
Competitive inhibiters- so similar to the substrate that they enter the active site and barricade the substrate from adhering with the enzyme. This can be reversed by adding more concentration of the substrate.
Non-competitive inhibiters- attach to a different portion of the enzyme and do the form to alter so the substrates cant bond right
Allosteric sites- some enzymes have allosteric sites a ways off from the active site. When substrates attach to it they can suppress or imitate enzyme activity. Adhering an activator to an allosteric site stabilizes the proteins conformation and leaves all active sites unfastened. Adhering an allosteric inhibitor stabilizes inactive signifiers of the enzyme.
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