BIO 277 01- Exam 1 (Unit 1 objectives)

Quaternary protein structure

>1 protein linked together. Ex: hemoglobin with 4 subunits. Same bonds as tertiary structure.

Active transport- primary and secondary active transport

Active transport= solutes move against their concentration gradient from an area of LOW to HIGH concentration.Membrane proteins are ALWAYS required Primary active transport= requires ATP (ex: Sodium-Potassium ATPase) Secondary active transport= energy of ion gradient (usually Na+) used to move 2nd solute. moves solutes against their gradient by using the energy of another solute gradient.

Role of Krebs cycle

Completes oxidation to produce NADH and FADH to enter the electron transport chain

Nucleic acidss

DNA, RNA- code for proteins- made up of nucleotides adenine, thymine, guanine, cytosin, uracil Other nucleotides= ATP, ADP, NAD, FAD

Draw a graph of rate of diffusion across a membrane as function of solute concentration for both simple and facilitated diffusion

Facilitate transport does become saturated and reaches a max where it levels off. This is because just like an enzymes all the available transporters are occupied at this (substrate), so this is the faster possible transport-rate

Define saturation of a transporter and be able to label this on a graph

Saturation= all available transporters are occupied. The part of the graph is the leveled off part.

Nucleus

Transcription here (DNA-> mRNA) Contains the nucleolus which synthesizes ribosomes.

Central Dogma of Molecular Biology

Transcription: DNA to mRNA Translation: mRNA to protein DNA-> RNA-> Protein

Def. transcytosis

Transcytosis= transport into, across, and then out of cell

Explain how the 3D shape of a protein determines it's functions

Weaker bonds fall apart easily with changes in pH and temperature. Ex: hydrogen, ion, van der waals bonds are weaker and are in secondary/tertiary structure.

Carbs

monosaccharide= glucose- stores chemical energy in covalent bond disaccharides= sucrose polysacchride= starch, glycogen- storage

Lipids

non-polar (hydrophobic) types tricglycerides (glyerol and 3 fatty acids) steroids (estrogen, testosterone) cholesterol (in membranes) phospholipids (phospholipid bilary)= ampipathic--> polar phosphate head and non-polar tails

Ionic bond

charged atoms that have lost or gained an electron. (Na+ and Cl-)

law of mass action

chemical law stating that the rate of a reaction is proportional to the concentration of the reacting substances. ** use the balance beam to find which way the reaction would go

Describe anabolic reactions involving carbs, lipids, proteins

enesis= building up glycogenesis= glucose-> carbs (glycogen stored) lipogenesis= glucose, fatty acids, amino acids-> fats protein synthesis= amino acids-> protein

Golgi apparatus

finishing school for proteins- mainly those for export out of the cell

Secondary protein structure

first degree folding. Alpha and beta pleated sheets hydrogen bonding

Proteins

amino acid (monomer) joined by COVALENT BONDS (specifically PEPTIDE BONDS)= primary structure secondary/tertiary= 3D shape- mainly ionic and hydrogen bonds (affected by temperature, pH) Examples: enzymes, receptors, signals (ligands)

Explain the difference between anabolism and catabolism

anabolism= building molecules, you are recently fed and storing energy catabolism= breaking molecules down, you are fasting and using stored energy

Covalent bond

atoms share electrons. STRONGEST type. (ex: carbon atoms in glucose, O2, water molecules)

Gap junctions

ion traffic windows- allow for propagation of action potential from one cell to the next (heart cells, smooth muscle cells of intestines)

Describe the structure of an ion channel and the different gating mechanisms

ligand-gated ion channel= ligands (signals) can bind with the gate to open/close it voltage-gated

Roles of electron trnasport chain and oxygen in the production of ATP

lksjf

Types of cell junctions- Leaky

lots of traffic between cells (hepatocytes-liver cells)

Role of reduced coenzymes

redu

Rough ER

ribosome-studded. Translation here (mRNA-protein) these are proteins usually for export out of the cell. Proteins made on free ribosomes stay in the cell.

Primary protein structure

sequence of amino acids covalent bond (peptide)

Smooth ER

steroid-hormone and lipid synthesis (anabolism) and break down (catabolism), site of calcium storage- calcium release related to cell activity

adherens junctions

strength eg. myocardiocytes (heart cells)

Define Homeostasis

the ability of the body to maintain a relatively stable constant internal environment. DOES NOT MEAN equilibrium (instead requires disequilibrium) keeping conditions static (instead within limits)

Tight junctions

very little traffic between cells- prevent leaks (skin, blood brain barrier, some kidney cells)

van de waals forces

weak, non-specific interaction between the nucleus of one atom and the electrons of another- allows molecules to pack closely together (phospholipid molecules)- bond is weak because if the atoms get too close their electrons repel each other

Tertiary protein structure

3rd level of folding. shape of protein held by hydrogen, ion, van der waals bonds)

oxidative vs substrate level phosphorylation

Oxidative= SLOW, but 34 ATP is made, NADH and FADH are used to create hydrogen gradient that provides energy to power addition of P to ADP Substrate= FAST, 6 ATP is made, glycolysis +Krebs, kinase enzyme removes a phosphate from molecule + adds to ADP

Hydrogen bonds

a weak attraction between a hydrogen atom and oxygen, nitrogen, or fluorine atom. (ex: attraction between water molecules)

Describe catabolic reactions involving carbs, lipids, proteins

olysis= breaking down glycogogenolysis= carbs-> glucose lipolysis= fats -> fatty acids and glycerol Proteolysis= protein-> amino acids Gluconeogenesis= amino acids-> glucose

Mitochondria

site of most ATP synthesis, contains enzymes of the Krebs cycle and electron transport chain

Explain how exchange of matter occurs between ICF, ISF, and plasma

CO2= ICF-> ISF-> Plasma-> lungs-> leaves body O2= lungs->plasma-> ISF-> ICF

Role of glycolysis

Glucose is broken down into 2 pyruvate in the cytosol. Makes 2 ATP

Water distribution in ICF, ISF, plasma

ICF= 67% ISF= 25% Plasma= 8% Extracellular fluid= 25%+8%= 33%

According to the law of mass action if you have more reactants than products. Would the reaction go forwards or backwards?

If you have more reactants than products the reaction would go forwards making more products to achieve equilibrium.

Be able to draw normal concentration gradients across a cell membrane for potassium, sodium, calcium, and protein

More Na+, Ca++ outside cell More K+, Proteins inside cell

Define an ion

a charged atom that has lost or gained electrons. (ex: Na+)

similarities/ differences between simple diffusion, facilitate, osmosis

similar- they are all passive transport requiring no energy simple diffusion= SOLUTES move from high to low concentration Facilitate diffusion= REQUIRES transport protein (ex: glucose, movement of water through aquaporins) Osmosis= WATER moves from area of high concentration to low concentration (or from LOW solutes to HIGH solutes). Also considered facilitated diffusion