Anatomy Polymers
glycogen (polysaccharide)
(animal starch b/c storage): if you eat too much glucose the pancreas sends message to the liver to pull it out of the blood stream and they are hooked together to form glycogen. This maintains homeostasis and the liver and muscle cells store it because they require the most energy and can then break it down into glucose for ATP; by hooking glucose molecules together it removes water molecules making it easier to store
catobolic
(catastrophe) takes big molecules and breaks them down
unsaturated fatty acid
(oil); take away some hydrogens, not straight chain, kinked, double bond b/w carbons where missing H, plants, molecules farther apart aka liquid so better for you
types of carbs
-monosaccharides= simplest sugars and a monomer -disaccharides= two sugar molecules together -polysaccharides= multiple sugars joined together in long chains
three types of RNA
1. mRNA: carries the "recipe" for a protein from DNA to the ribosome 2. tRNA: brings specific amino acids to the ribosome for addition to growing protein 3. rRNA: major structural component of ribosomes
chromosome vs chromatin
1. ready to divide, tightly coiled vs 2. uncoiled, in nucleus, doing its job
triglyceride
3 fatty acids
monomers of RNA
5C sugar, phosphate group, nitrogenous base
purines
A,G
nitrogenous bases of RNA
Adenine (A) and Uracil (U)=double bond; Cytosine (C) and Guanine (G)= triple bond
nitrogenous bases
Adenine (A) and thymine (T)= double bond; guanine (G) and cytosine (C)= triple bond
pyrimidines
C,T
two types of nucleic acids
DNA (deoxyribonucleic acid) and RNA (ribonucleic acid)
glycerol
a three carbon molecule
hydrogenated
add hydrogen to unsaturated means straightens kinks out... makes saturated
secondary protein structure
alpha helix and coil of amino acid chain. Bends primary structure into an alpha helix or beta pleated sheet held together by side groups *need side chains to hold coil in place for alpha helix* *interactions among side groups must be in place for beta pleated sheet*
monomers of proteins
amino acids: 20 different amino acids are bonded together to form thousands/millions of different kinds of proteins in living things in different combos and sequences
nitrogen important because
amino group in amino acids
every amino acid has...
amino group on L and carboxyl on right
why does membrane have to be a bi-layer
b/c water on both sides and hydrophobic tails wouldnt like it so we get semipermeable membrane (H20 can move in and out despite hated area)
how is energy from polysaccharides harvested?
broken down by digestive process into monosaccharides which will be used by cell to make ATP
monomers
building blocks for polymers made up of subunits
dna replication bubble
can open up in multiple places to save time
saturated fatty acid
cant hold any more hyrogens then already does, straight chain, glycerol and fatty acids, fat, atoms closer together so (semi) solid at room temp, no double bonds
example of enzyme
catalase breaks down hydrogen peroxide (H2O2) which is a normal byproduct of chemical reactions but is toxic to cells and takes a lot of time to decompose to H2O and O2...one molecule can break down 40 M molecules of H2O2/sec
in plants vs fungi
cellulose for cell wall vs chitin for exoskeleton (and dissolvable structures for medical procedures)
lipids
diverse hydrophobic molecules made up of monomers BUT NOT POLYMERS LIKE OTHER BIOMOLECULES...commonality is no affinity for h2o
carbohydrates
energy molecules that include sugars and their polymers; body's first source of energy but dont use directly... they take energy out of bonds to transform it into ATP
lipids used for
energy storage (1 gram of fat contains twice as much energy as gram of carb), insulation (layers of fat under skin to conserve heat), protective coatings (cell membranes as phospholipids), cushion (against physical or mechanical injury to internal organs and structures
why animals have fats and not oils
fats solid @ room temp. and therefore if obese liquid>fat would be gross and wouldn't be able to move effectively...plants dont move.
micelles
formed when added to water (droplets)
monomers of lipids
glycerol and fatty acids
explain phospholipid structure
hydrophilic head made of phosphate, choline, and glycerol, hydrophobic tail that is kinked with both saturated and unsaturated chains
glycoprotein
identity proteins that have a carbohydrate chain on outside that identifies who they are (ID tags)
cholesterol
important part of membrane; keeps phospholipid tails from sticking together and gives flexibility and stability to membrane
structural functions
in hair, nails and claws; acts as enzymes ie catalase for H2O2 which is toxic for cells so breaks it down
tertiary protein structure
involves folds and large loops, has polypeptide backbone, hydrophobic interactions, disulfide bridges, and ionic bonds, hydrogen bonds make loops
What are polymers
large molecules consisting of many identical or similar subunits linked together
steroids
lipids consisting of four fused rings with various side groups
difference b/w monomers of carbs and proteins vs lipids
lipids have 2 monomers: glycerol and fatty acids join for 1 polymer
fatty acids
long straight chain of carbon atoms both saturated and unsaturated
structure of DNA
long, double stranded molecule, double helix with coding side (read by mRNA) and non-coding side, double stranded for protection from breakage, sugar-phosphate backbone, codes for proteins and one gene=one trait=one protein
what are id proteins good for and bad for
macrophages destroying bacteria b/c know what it is and bad for organ transplants b/c easy to reject
fats
made by animals, solid or semi-solid @ room temp, saturated, ie. butter, lard, fat on meats
oils
made by plants and fish, liquid @ room temp, unsaturated, ie cod liver oil and olive oil
DNA monomers
made up of 5C sugar, phosphate group, and nitrogenous base to make up a nucleotide
dehydration synthesis
monomers are linked together by removing a water molecule ANABOLIC
which are functional
not primary, secondary; most only functional with tertiary
what else has double phospholipid bilayer
nucelus
divided into two groups
oils and fats
peripheral proteins
on outer edge (sides)
monoglyceride
one fatty acid plus glycerol and usually on 1st carbon
trans configuration
opposite side= straight molecule
bond between amino acids
peptide bond
hydrolysis
polymers are disassembled into their monomers by a process that adds a water molecule
enzymes
proteins that act as catalysts (substances that speeds up chemical reactions rate what WITHOUT taking part in the reaction); lowers activation energy needed; required for almost all chemical reactions that happen in living things
more about DNA
provides info for own replication, allows info to be passed on to next generation, directs RNA synthesis thereby controlling protein synthesis, found in nucleus of cells except when nuclear envelope breaks down during mitosis and meiosis
dehydration synthesis of disaccharides
put together by removing water molecules from side chain of H and OH
cis configuration
same side=bent molecule
primary protein structure
sequence/chain of amino acids made up of peptide bonds
fluid mosaic model
so many components and MOVEMENT; cholesterol, transmembrane proteins, glycoproteins
transmembrane proteins
span inside and outside and help molecules diffuse through w/ facilitated diffusion. ie glucose
phospholipids
specialized lipid molecules that have only two fatty acid chains instead of three (diglyceride); the third OH group is attached to a phosphate (P4); both hydrophobic and hydrophilic behavior towards H2O
examples of polysaccharides
starch (storage) in plants and cellulose
cholesterol as a steroid
steroid from which other steroids are made including sex hormones
hormones and examples
substances (not all proteins ie steroids) produced in one organ of the body and sent to target another organ ex. testosterone (testes to muscles and leads to broad shoulders, adams apple, more muscular) and estrogen (ovaries lead to hour-glass figure, breasts etc)
induced fit of enzyme
substrate in active site of enzyme...hug;)
example of disaccharide
sucrose (glucose and fructose) and maltose (glucose and glucose)
specific for what
temperature, pH, substrate...denatures if not optimal
proteins
the most numerous molecules in body and have many functions: contacting muscle fibers (actin and myosin), transporting oxygen (hemoglobin), providing immunity (antibodies), regulating other proteins (hormones)
diglyceride
two fatty acids plus glycerol, usually on 1st 2 carbons
quaternary structure
two or more tertiary structures put together to form a protein
energy of activation
two reactants... same products and up with same amount energy at end...different amount of time