chemical energy from eletron transfer is converted to what?

heat energy

Proton pump

Energy of electron transport

pumps proton across membrane

stage 1

Proton Influx

Proton gradient

Harnessed by ATP synthase

Makes ATP

Stage 2

Mitochondria

Catalyze major conversion of energy  

Matrix

Inner membrane

Outer membrane

Intermembrane space

Matrix

enzymes

oxidation pyruvate and fatty acids in citric cycle

Inner membrane

folded - cristae

proteins carry out oxidation of ETC

ATP synthase (inner) = make ATP (in matrix)

Outer membrane

porin protein (channel forming)

permeable to molecules of 5000 daltons or less

Inner membrane

enzymes

use ATP from matrix

phosphorylate nucleotides

NADH

donate electrons to ETC

 Ubiquinone & Cytochrome C

carry electrons from one enzyme complex to another

ATP synthase

reversible coupling device

electochemical proton gradient to chemical bond energy

vice verse

Reduction

uses H from water

Oxidation

Releases H to form water

Quinones

carry electrons within lipid bilayer

Redox Potential

increases along mitochondrial ETC

Proteins

building block for cell assembly

make up dry mass

enzymes, structure, transport, motor, signal, etc.

Shape and Structure of Proteins

polypeptide chains

20 amino acids determine folding

amino acids linked by covalent peptide bonds

Non-covalent bonds

Electrostatic attractions

Hydrogen bond

Van der Waals attraction

van der Waals force

attraction btwn electron rich region on a molecule and electron poor regions of anothe molecule

seen as electric dipoles

molecules cohere

surface tension & capillary action

Hydrophobic forces

help proteins fold into compact conformation

hydrophobic core region of proteins

contain non polar side chains

hydrophilic regions of protein

outside polar side chains

which can hydrogen bond

Hydrogen bonds

help stabilize proteins fold and shape

backbone to backbone

side chain to side chain

back bone to side chain

Urea

denatures protein

but

once removed protein goes back to conformation

Misfolded proteins

can damage cells and tissues

Ex. prion proeins

diseases: encephalopathy

creutzfeldt-jacob disease

Kuru

Common folding patterns

alpha Helix

beta pleated sheet

Alpha helix

intramolecular hydrogen bonding

btwn functional group of same molecule

segment can cross a lipid bilayer

beta-pleated sheet

intermolecular hydrogen bonding

weak forces btwn neighboring atoms

2 forms: parallel & antiparallel

Coiled-coil

Serine proteases

Proteolytic enzymes

Dimer

Single protein subunit shapes

spherical shell

filament

tube

stabilize favored protein conformation

interchain (two units)

intrachain (S-S btwn one unit)

releases 60Kcal/mole

very specific

folded protein = binding site

chaperone helps with folding

interact with ligands

Y shaped Protein

right side - light chain (changes)

left = heavy chain (constant region)

top of Y - antigen binding site

disulfide bonds

light chain

catalyze polymerization rxns

DNA & RNA

A. binds two molecules close to ensure rxn

B. Rearranges electrons of substrate to create partial pos & neg charges to ensure rxn

C. enzyme strains substrate forcing it to transition state to ensure rxn

product of one rxn becomes substrate for the next

end product of pathway reacts with begining enzyme to shut off the pathway

occurs on the allosteric site = product shuts off active site

(conformational change)

negative regulation

Positive feedback

amplifying and moving away from target set point

(ripening of fruit, 1 bad apple spoil whole bunch)

spread signals

quick

Negative feedback

closer to set point-stabilized

ex. body temp.

Serine + Protein kinase

ATP to ADP

Active form Serine

Serine phosphorylated + prtein phosphatase

Rmove Phosphate ion

Serine off

turn proteins on

fast

hydrolyzed form of GTP

slow

turns protein off

powered by ATP hydrolysis

moves one direction

Ion exchange

Gel filtration

Affinity- purification of proteins through ligand bonding

SDS polyacrylamide gel

Isoelectric gel

2-D gel electrophoresis

Sonication sounds wave to break open cells

Differential centrifugation & 

Buoyant Density centrifugation

 for proteins with charges

separate based on charge

dissolve according to weight

sds = detergant denature and neg charge

neg to positive end

generate pH gradient

isoelectric point -pH at which molecule not charge = stop moving

sep in tube gel by isolectric point

stop at neutral

then sds gel

spots in gel unique

low speed cetrifuge for pellet of large cells

high speed further separate larger cells (ribosomeS)

not pure

Buoyant Density centrifugation-

involved in cell comunication

import and export

cell growth

motility

move in plane - lateral

flex and rotate

rarely flip

stiffens cell membrane

polar head

steroid ring rigid

non polar hydrocarbon tail

play role in synth. lipid bilayer

transfer new lipids to bilayer

transport

anchor

receptors

enzymes

Na+ pump

Na out and K+ in

Integrin

link intracell actin filaments to extracellular matrix protein

plated derived growth factor (PDGF) receptor

adenylyl cyclase

cat. production of intracell signaling cAMP in response to extracell signals

Transmembrane-alpha helices

monolayer

lipid linked

protein attached

proteins in bilayer have lateral movement

can dissolve proteins

SDS - polarized

Triton X-100 - non-ionized/polar at hydrophilic end

transfer one molecule across membrane

glucose

transport 2 diff molecules in same direction

Lactose Permease mechanism

transfer two molecules in opposite directions

ADP/ATP

conformational change to release

Na+ K+ pump

ADP imported into mitochrondrial matrix

ATP exported out into cytosol (intermembrane space)

carrier proteins which use energy to move molecules

3Na+out

2 K+ pump in

1 atp

bind messanges to change permeability

activate enzymes

trigger other messangers