test 2: cahpter 5

what are the four macromolecules

1. carbohydrate

2. lipids

3. protein

4. nucleic acid

carbohydrate

lipid - triglycerides

lipid - phospholipid

lipid - steroid

protein

nucleic acid

carbohydrates

sugars/saccharides

carbohydrates: structure

• 2 basic types - complex and simple

• built with carbon, oxygen, hydrogen

• can be linear or loop into rings

carbohydrates: function

• helps cells with atp production

• quick energy

• build plant cell wall

• build insect exoskeletons

monomer vs polymer - monomer

• a building block of a molecule if complex form is built with repetition

• building block for a complex molecule but the cpmplex molecule has to be built with repetition

  • monomer is also molecule

monomer vs polymer - polymer

• complex form built through repeated addition of an unit

• linked end to end with covalent bonds

dehydration synthesis

• when -OH from one molecule leaves and -H from another leaves to form one big fat H2O molecule. the 2 molecules then bond together to form 1 larger molecule

hydrolysis

• OPPOSITE OF DEHYDRATION SYNTHESIS - reverses it

• a larger molecule breaks into 2 smaller ones by adding pieces of H2O (-OH to one and -H to another) after breaking a bond within the mol

• soooo hydrolysis is when water self inserts itself by breaking a larger molecule into two smaller ones and there is an extra -OH or -H in it

  • ex for triglyceride, it splits it apart back to its componenets (glycerol and its fatty acids)

carbohydrate: how can dehydration synthesis and hydrolysis can be used to build and break down carbs

dehydration builds carbohydrates because it removes a water molecule so a sugar link can form

hydrolysis breaks them down because it adds water to split the bonds soooo no more sugar links

lipids: structure

• nonpolar

• trans-fat

• saturated fats

• built with a lottt of carbon and hydrogen, a little oxygen

THREE TYPES

• triglycerides

• phospholipids

• steroids

lipids: function

• 1 insulation

• 1 energy storage

• 1 cushions organs

• 3 chemical messengers

• 2 cell membrane structure (phospholipid bilayer)

1- triglyceride - energy stroage

2- phospholipids - cell borders

3- steroids - chemcal signals

lipids: triglycerides; what is glycerol

• built by connecting 1 glycerol and 3 fatty acids

• non polar - doesnt have polar hydroxyl groups so cant bond

glycerol

• considered a monomer because there is no repetition of a unt

to build one triglyceride, dehydration synthesis needs to occur 3 times, once for each fatty acid

carboxyl group - O=C-O-H

hydroxyl - O-H

lipids: saturated vs unsaturated fats - saturated

saturated

• straight and crammed together of hydrogen atoms, solid

• all c to c bonds are single with max amount of h

• no double bonds

• solid at room temp

• increased LDL and decreased HDL because they impact cells ability to absorb

LDL - low density lipoprotein

HDL - high density lipoprotein

lipids: saturated vs unsaturated fats - unsaturated

• kink so hydrogen atoms cant pack together, more “liquid“

• one or more C=C/ -=C and a deceased amount of H

  • double bond = lose hydrogen

• double bond = kink

• healthier

• liquid at room temp

• less “stackable“

polyunsaturated

• goood for you, less hydrogen

• 3 or more C=C/C-=C bonds in fatty acid chains

hydrogenated

• bad for you, more hydorgen

• man made saturation of unsaturated fats by H bombardment that breaks C=C/C-=C

trans fat

• when a cisisomer is altered and flattened, making its shape something the body can’t process

• trans = hydrogen is across / opposite sides

phospholipids

• made up of a phosphate group, glycerol, and fatty acid chain

• r group has nitrogen atom

• contain carbon, hydrogen, oxygen, phosphorus, and nitrogen

• make up cell membrane

• polar head and two non polar tails

  • phospahte group (head) is polar so likes water

  • fatty acid tail doesnt like water so hydrophobic region of cell membrane

• kink is double bond and unsatured fatty acid

• 
  

• modified triglyceride because 1 chain is swapped

• hydrophillic head → charge from choline and phosphate group that allow interactions with aqueous head

• hydrophobic tail - fatty acid chains that are C/H annnd non polar

the red white thing is cell membrane

steroids

• four rings

• used as chemical messengers and structural component of cell membrane

cholestrol

• fluidity of cell membrane

cortisol

• stress = high cholestrol

estradiol (estrogen)

• 
  

triglyceride storage ; brown fat vs white fat

• location varies on sex, genetics and activites

• adipose tissue with adipose cells/adipocytes

  • when fat increases, adipocytes increase in size

brown fat

• extra blood vessels in babehs because they cant shiver so temp regulation

white fat

• normal fat, used for energy storage

protein

• amino acids are building blocks (monomer)

• unfolds and loses shape due to changes in pH and temperature

• can misfold

• built with help from ribosomes

protein : function

• structure = function

• active transport

• enzymes (catalyst)

• signaling

• repair

protein: The 3 different types of side chains and their impact on final shape

R GROUPS

1. nonpolar and hydrophobic

• hate water

• hide from water by bundling together tightly in the very center of protein

2. polar and hydrophilic

• love water

• push themselves to the outside surface of the protein so they can touch the watery surrounding, holding parts of shape togetehr like velcro

3. charged and hydrophilic

• carry positive or negative elctrical charges

• opposites attract. posoitve attract negative and loops of protein lock into place

protein: building a protein; structure again

has

• amino group

• carboxyl group

• variable group

• central carbon

protein: hydrosynthesis

• peptide bond forms

• building the chain will happen in a ribosome

four levels of protein organization

1. primary

• chain of amino acid

• determined by dna

• change one amino acid, entire protein fails

• stabilized by peptide bonds. covalent bonds

2. secondary

• repeating

• shape are folds and helixes

• stabilized by hydrogen bonds because polar r- group

3. tertiary

• folded chain folds even more to an unique 3d shape

• stabilized by

  • hydrogen bonds polar

  • ionic bonds charged

  • other van der waals any

  • disulfide bridges polar

  • hydrophobic interaction

4. quaternary

• two or more tertiary polypeptides combined to form a functional protein with a unique 3d shape

chaperonin

protects an unfolded protein until it can fold into proper 3d shape

• 
  

enzymes

• enzymes are very specific, each enzyme only catalyzes one exact reaction

  • lock and key, enzyme is lock and molecule (substrate) is key

• speed up chemical reactions

  • lower the energy required to make molecules react

    • build (anabolic)

    • break (catabolic)

• as a protein, enzymes can unfold if pH or T changes

• inhibitors - molecules turn anzymes off, block active site (the enzyme)

  • non inhibitors change shape of enzyme itself

nucleic acid

• DNA

• RNA

  • mRNA

  • tRNA

  • rRNA

nucleic acid: structure

• base: c, t, g, a, u

• monomer is nucleotide

• single or double helix

• sugar - deoxyribose vs ribose

• backbone - phosphate group and sugar

• built with help of enzymes

nucleic acid: functions

• express genetic information - has instructions that allow for building of proteins

dna structure

• double helix

• a=t and c=g

  • a and g is purine nitrogenous base

  • c and t and u in rna are pyrimidines

• antiparallel

  • one side is 5’-3’ and its partner is 3’-5’

hydrogen bonds

• outer backbone is strong covalent bonds, bases in middle are bonded with weak hydrogen bonds

  • do this because think of the bases like a zipper, you can unzip it down the middle sooo cellular machinese can come and copy it