English Class 250 College Most Important Data

Extremely important Data

Cell Theory

1. all organisms are composed of 1 or mroe cells

2. all cells are from prexisting cells

3. cells are the structural unit of life

complex features

complex features: structure, composition, metabolism

3 Domains of Life

Eukarya, Archaea, Eubacteria

Prokaryotes

Archaea

Eubacteria

Eukaryotes

Animals

Plants

Protists

Fungi

Things ONLY Eukaryotes have

1. Has nucleus

2. Has chromosomes and 1+ copies

3. Membrane bound organelles for respiration/photosynthesis.

4. Cytoskeleton w/ motor proteins

5. Cell wall made of cellulose or chitin

6. Mitosis and Meiosis

7. 3+ RNA polymerase

8. Sexual reproduction

9. Vesicles (take particulate matter)

Transmission Electron Micrograph

uses beam of electrons to scan charge of sample

microtome: made of diamond, slices cell into thin slice

sensor: scans charge from bottom

• darker = more electrons

X-Ray Crystalogy

takes pics of proteins that are crystalized

• can crystalize proteins easily by sending them to space

• creates a defraction patterntoscan

Light Microscopy

• uses lens and light to magnify a sample

• can use dyes

Prokaryote Eukaryote Similarities

1. Plasma membrane construction

2. gene code

3. gene expression: transcription and translation

4. ATP

5. both translate/insert proteins into the membrane

6. proteasomes are similar in Archaea and Eukaryotes

Order of outer cell

Cell wall (not in animals) —> Cell Membrane —> Cytoplasm

Plasmodesma

Pore that connects neighboring plant cells and used for communication

• salad bar

Nucleolus

assembles ribosomes

• is inside the nucleus

Ribosomes

Site of protein synthesis

• can be imbedded in Rough ER

Smooth Endoplasmic Reticulum

Synthesizes Lipids

Rough Endoplasmic Reticulum

• Has ribosomes that make proteins

Vesicle

Stores and Transports (circle bubble things)

Golgi Complex/Apparatus

• DOES POST SECONDARY MODIFICATION OF PROTEINS

  • sticks lipids

  • adds sugar

  • splice

  • synthesizes cell wall compounds

Peroxisomes

Oxidates for chemical reactionsV

Vacuole

takes up space, a bunch of water

Microtubule

Gives shape of cell

allows movement of materials in cell

Proteasome

Recycles proteins and breaks them down into Amino Acids (AAs)

The AAs are reused for new proteins

Secretory Vesicle

Emerges from Golgi

• Transports/Stores

  • Part of endomembrane system

Endosome

brings macromolecules inside cell to eat

• endocitosis: formation of endosomes

Lysosome

In animal cells only

• safe space for hydrolosis

• 2 ph, acidic bc proton pumps on outside

Hydrolosis

reaction where a H2O is used to break down a molecule

Cytoskeleton

1. Intermediate filaments: fibrous protein for structure. Isn’t shared. Runs everywhere in the cell.

2. Microtubules and Filaments: Used in Mitosis, use actin

Centrosome

Specialized microtubule organizing Complex (MTOCS)

• Creates microtubules for mitosis

Glycogen

Commons source of Carbhohydrate energy

Animals vs Plants for energy storage + usage

Animal: glycogen, lysosomes

Plants: starch chloroplasts

Both: have mitochondria

Model Organisms

1. E coli

2. Fruit fly

3. Mouse

4. Nematode

5. Yeast

6. Mustard Plant

Units used for Cell Size

Milimeters: 10^-3

Micrometers: 10^-6

Nanometers: 10^-9

Cell Size is limited by:

1. Vol of cytoplam… too big to translate DNA

2. if too much volume of cytoplasm, there wont be enough nutrients

3. diffusion is slower with more cytoplasm

Macromolecules

1. Carbohydrates

2. Nucleic Acids

3. Lipids

4. Proteins

Carbohydrates

Monomer: monosaccharide

Polymer: disaccharides, polysaccharides, oligosaccharides,

Monosaccharides

Means “One Sugar”

• water soluble

• can build glycerol

• Ex) ribose + deoxyribose

• CONTAINS CARBONYL (ALDEHYDE OR KETONE) AND 1+ HYDROXYL

• form rings in Aqueous solutions

Glucose vs Fructose

isomers but very different

fructose —> in liver, turns to fat (bad msot of the time)

glucose —> energy

Monomers

Monosaccharides

• dehydration: disaccharides, oligosaccharides, polysaccharides (hydrolosis to break back down to monomers)

Fatty Acids + glycerol

• polymers: triglycerides + phospholipids

Nucleotide

• Nucleic Acids

Amino Acids

• polypeptides

Alpha vs Beta carbon structure

• depends on orientation of hydroxyl group (OH)

Alpha: OH pointing down from ring (goin down onh im)

Beta: OH pointing up (erect)

Carbohydrate Polymers

• made up of monosaccharides (cyclic) using glycosidic linkages (attatched via dehydration rxn).

Disaccharides

2 monosaccharides joined by glycosidic linkages

ex) Maltose: 2 glucoses, maltase enzyme to break it down

Lactose: glucose and galactose

Sucrose: glucose and fructose

Polysaccharides

Made of 1 or more ring types

• can be branched or unbranched

• formed via dehydration

• broken by hydrolosis

Oligosaccharides

smaller polysaccharides

• used in protein modifications

• in lipids

Amylose/Amylopectin

Starch, used to store energy in plants.

• 1-4 alpha linkages

• amylase: can break it into glucose/maltose

Amylopectin: plant energy storage easy to digest

• alpha 1-4 linkages; alpha 1-6 linkages for branches

Glycogen

• Highly branched (not linear)

• Has glycogenine (enzyme) in the center that can be used up, which is rare for enzymes

• Linkage: alpha 1-4

  • branches: alpha 1-6 linkages

• Location: muscle/liver : blood sugar and ATP for movement

Cellulose

• Made of Beta glucoses

• insoluble

• Linkage: Beta 1-4 Linkages

Chitin

Nitrogen and acetate groups attached to glucose

Linkage: Beta 1→4 Linkage

• exoskeletons: bug and fungi

Lipids

• Oily macromolecules

• Hydrocarbons, nonpolar: insoluble!!!**

• Has carboxyl group at end which is hydrophilic

Function: Energy storage, membrane structure, coating

Alpha carbon: carbon next to carboxyl group

Omega carbon: carbon of methyl group (CH3)

Saturated Fat:

Single bonds, maximum amt of hydrogen bonds in tail

Oleic Fatty Acids

is monosaturated: one double bond

Beta Oxidation

metabolic breakdown of fatty acids

Polyunsaturated Fatty Acids (PUFA)

• More than one double bond (poly-unsaturated)

• have different functions based on position of the double bond near omega carbons.

• ex) Omega 3 fatty acid: Double bond 3 carbons awa

  • DHA

Tri-glycerol

• Common PUFA for Energy Storage

  • 3 carbons w/ a hydroxyl (OH) group on each.

• 3 fatty acids bound to a glycerol!!!!!!!!**

• Nonpolar!!! bc hydroxyls esterify when bonding to a fatty acid

• 
  

Phosphoglycerides (Phospholipids)

• Made up of: 2 fatty acids, 1 phosphate group, glycerol

• Has hydrophillic head: has negative phosphate and choline

• Amphipathic: Both nonpolar and polar

• 
  

Structures of phospholipids In Water

1. Phospholipid Bilayer: hydrophobic tails — Hydrophillic heads. Seperates water

2. Micelle: Circular singular layer. Transports cholesterol

Sterols

backbone of 4 carbon rings but has no fatty acid tails

Cholestrol

mostly nonpolar, sticks to hydrophobic tails in lipid membrane.

• Maintains viscosity of the membrane

made in animals, modified into testosteron and estrogen and vitamin D

Nucleotides

• monomer of Nucleic Acid

has phosphate group, 5-Carbon Sugar, and a Nitrogenous Base

ex) ATP

Nitrogenous Bases

Adenine, Guanine, Uracil, Cytosine, Thymine

Nucleic Acid

• polymer, stores genetic info

DNA

RNA: reads DNA at 3’ to 5’

• single stranded

• Can fold into 3d structures (RIBOSOMES! rRNA)

• RNA enzyme: ribozyme

Protein

• polymers of AAs, diverse functions bc functional groups

• AAs are bonded via peptide bonds

Amino Acids

• have a alpha carbon, ammine group (+), carboxyl group (-), and a R group attached to alpha carbons.

  • R groups: variety of them, can be polar charged/uncharged/nonpolar

• have peptide bonds btwn eachother → polypeptide chain → protein

Peptide bond

Bond btween AAs

• Form between alpha carbonyl and alpha amino of AAs.

tRNA + How does Hydroxyl group get lost during tranpsorting?

bring AAs to ribosome via covalent bond

How does Hydroxyl group get lost during this?

1) Activation: Adds energy. ATP reacts from amino acid to atp.

• PPi is replaced, AA goes to AMP which adds energy…??

2) TRNA has: anticodon, and a terminal adenine end

• Performs dehydration RXN WITHOUT a h2O***

  • AMP-AA becomes AA-tRNA

    • takes oxygen and an OH is lost, so we lose a h2O basically without one being there

Amino Acids Composition

• R groups are hydrophobic (van der waals)

• doesnt have N or O

• size and shape variess

• 
  

primary structure

sequence of amino acids in the polymer (shape of protein)

secondary structure

Conformation of adjacent AAs into alpha helix, beta sheet, hinges, turns, loops.

!!! Results from H bonds from Amide Linkages !!!

• only h bonds

Teritary Structure

the conformation of the entire polypeptide.

• It is stabilized by noncovalent bonds.

• Proteins can be fibrous or globular.

• Staiblized via non covalent bonds

• all kinds of bonds bc it pertains to the whole polypeptide (r groups), so wide range of bonds

• Fibrous or globular proteins

• Ribbons like

WHY??: we need exact 3d dimensions to undergo reactions

ex) myoglobin

Quaternary Structure

conformation of 2+ polypeptide chains

Protein Domains (Motif)

occur when proteins are composed of two or more distinct regions.

• Each domain is a functional region

• We can exchange/reuse them bc they have functions already

• Protein families: evolution

Protein Folding

• Steps/process of proteins assuming their conformation

2 Rules

1. Secondary Structures form first:

2. Hydrophobic Collapse occurs first in aqueous environment after 2ndary structures.

Molecular/Protein chaperones: prevent interactions during protein folding. Creates environment to prefer 1 rxn.

Membrane Functions

1. Compartmentalization

2. Scaffold for Biochemical Activities

3. Selective Permeable Barrier

4. Transporting Solutes

5. Responding to External Signals

6. Intercellular Interaction

7. Energy Transduction

Fluid Mosaic Model

• fluidity from LIPIDS! It moves laterally

• Cholestrol: hydrphobic except for hydroxyl which anchors to leaflet.

  • Keeps leaflets packed and provents soldification/too much movement/ viscoscity

• bilayer has proteins in it

Integral Proteins

• a part of Fluid mosaic Model, inbetween ig

• sometimes have a sugar attatched, which is called a glycoprotein

• different from peripheral proteins, which are located on the heads.

• attatched to bilayer assymetrically, distinguishes leaflets

• amphiphatic: hydrophobic anchor and hydrophylic functional domains outside bilayer idk man its just assymetrical

Sphingosine

• Apart of the sphingolipid Structure

• an amino alcohol with a long hydrocarbon chain

leaflets

the two layers of the phospholipid bilayer.

They are actually different and assymetrical, the heads diff shape

Glycolipids

havelonger carb chains (oligosaccharides) that may be cell-to-cell recognition sites (ANTIGENS).

• Covalent bonded to lipids on extracellular surface of bilayer

Peripheral Proteins

• attatched to membrane by weak bonds (non covalent bonds)

• easily solubilized

• On outside of bilayer on either the extracellular or cytoplasmic side

  • Signal transduction: moves info from one place to another

Lipid anchored membrane proteins

classified by type of lipid anchor and orientation

• uses n terminus and terminus

• N: ammine

• C: carboxyl

  • AAs have both

Glycoproteins

short, branched carbs for interations with other cells/structures outside

• uses ammine linkage (asparasine) or hydroxyl (serine, threonie)

aquaporin

regulates h2O in membrane. can go out and in and vice versa.

lipid raft

specialized regions of outer leaflet

• raft has two sides: outside and inside

outside: glycoplipids

inside: signal protein attatched to fatty acid

• sends signals/resposnes (similar to a functional domain in the fluid mosaic model)

• favorable for cell surface recptors