exam 1 concepts review

common body cations

Na+, K+, Ca2+, MG2+, H+

common body anions

Cl-, bicarbonate ion, phosphate ion

least to most electronegative

H, C, N, O (harry cooks nice omelets”

weird nonpolar intermolecular force

brief interaction between e- of np molecules adjacent

inter

between

intra

inside

waters role in the body

transport, lubricate, cushion, excrete waste

specific heart

calories needed for temperature to rise of 1g of a substance by 1c°

heat of vapor

energy needed for liquid to turn to gas for 1g of the substance

dissociation

ionic compunds

electrolytes

salts, acids, bases

non electrolytes

glucose

what is the product of h2o dissociating

H+ + OH-

mass/volume

mass of solute/volume of solution

mass/volume%

mass of solute/100 mL of souultion

molarity

moles of solute /L of solution

molality

moles of solute/kg of solvent

osmoles

the extent of the solution altering H2O movement through osmosis

osmolarity

number of particles in 1L of a solution

osmolality

number of particles in 1kg of H2O

macromolecules

Carb, lipid, protein, nucleic acid (CLaPiN)

macromolecules always contain

carbon, hydrogen, oxygen, nitrogen, phosphorus, sulfate (CHON P.S.)

macromolecules functional groups

hydroxyl, carboxyl, amine, phosphate

pyrimidines

c, u, t

purines

a, g

components of a nucleotide

phosphate group + nitrogenous base + ribose sugar

what bond connects nucleotides

phosphodiester bonds

protein functions

catalyze chemical reactions, structure support, body movement, transportation in blood, membrane transportation, protection

what makes an amino acid

amine + carboxylic acid + r group

polar amino acids

hydrocarbons + O, N, S

non polar amino acids

H or H-C

primary proetien bons

hydrophobic exclusion

secondary bonds

hydrogen bonds between protein r groups and amines. carboxylic acid functional groups.

tertiary

ionic bonds

quaternary

disulfide bonds between S-H groups

enzyme locations

in cell, embedded in plasma membrane, secreted from cells

inorganic cofactors

attached to enzyme and required for function

organic cofactors

not attached to the enzyme, specific functions for assisting

optimal enzyme pH

6 - 8

optimal temperature

37 C or 98.6 F is regular, 104 F or 40 C is max

atp pathway: substrate level phosphorylation

direct

atp pathway: oxidative phosphorylation

indirect

glycolysis reactants and products

r: glucose

p: 2ATP, 2NADH, 2 pyruvateq

glycolysis steps

1-5: invest 2 ATP to split G3P

6-7: create NADH and H+, add Pi. Pi transferred to ADP and becomes ATP

8-10: create an isomer. loose H2O. Remaining Pi is transferred to ADP to make ATP. Create pyruvate

how is glycolisis stopped?

ATP allosteric inhibitor turns of PFK

intermediate stage reactants and products

r: pyruvate and CoA p: 2NADH

intermediate stage steps

1. carboxyl released from pyruvate as CO2

2. energy released. 2H+ transferred to NAD+ to make NADH and H+

3. acetyl CoA goes into citric acid cycle

citric acid cycle reactants and products

r: acetyl CoA p: 1 STP, 3NADH, 1 FADH (per 1 turn, so x2 for each glucose)

citric acid cycle steps

1: form citrate with acetyl CoA oxaloacetate.

2-3: H2O removed from citrate and creates an isomer by reattaching the H2O

4-5: NAD+ is reduced w/dehydrogenase to turn into NADH. CoA is attached.

6: CoA removed and ATP is formed through substrate-level phosphorylation

7: FAD reduced to FAHD2 w/ dehydrogenase

8: H2O removed

9: NAD+ reduced to NADH. Oxaloacetate regenerated

note: now u have 6CO2???

etc reactants and products

r: NADH and FADH p: NAD+ and FAD

etc structure

in the cristae, H+ pumps, e- carries, ATP synthase enzymes. more H+ in the outer compartment than matrix

etc steps

1. e- transferred from coenzymes to O2. NADH or FADH2 releases H+ and is oxidized. e- is passed to O2. O2 and 4e- and 4H+ combined to make H2O.

2. H+ gradient established from falling e-. KE is harnessed by H+ pumps to move it from the mitochondrial matrix into the outer compartment.

3. H+ gradient harnessed to form ATP. H+ moves down the concentration gradient, then moved by ATP synthase from the outer compartment to the matrix. KE from falling H+ harnessed, forms bond between ADP + Pi to make ATP