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66 Cards in this Set

  • Front
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metabolism

chemical activity in organism

anabolism

building complex molecules from simpler ones with input of energy

catabolism

breaking complex molecules into simpler ones with output of energy

Isotopes

different atoms with SAME element with SAME # of protons but DIFFERENT # of neutrons

radioisotopes

radioactive atoms of element that DECAY into SMALLER atoms, SUBATOMIC particles, and ENERGY


radiation types: alpha, beta, gamma rays

Half-life

the TIME it takes for ONE half the nuclei in a radioactive sample to decay

The use of radioactive tracers in medicine:

1. recognize cancerous areas


2. helps in studys


3. in images of tumerous

Intramolecular bond

Ionic & covalent

ionic

non and metal


dissolves

covalent

two non metals


share electrons


do not dissolve



determine bond type

electronegativity: >1.7=ionic


<0.2=pure covalent


>0.2=polar covalent

intermolecular forces

london


dipole dipole


hydrogen bond

properties of water

1. solid floats on liquid


2. cohesive


3. adhesive


4. high heat capacity


5. universal solvent

acid

~ pH < 7


An acid is a strong compound which dissociates in water and releases hydrogen ions into solution~


Acid strength increases as pH decreases~ Acids increase the number of H+ ions in a solution

base

pH > 7


A base is a compound which dissociates in water and often releases hydroxide ions into solution~


Base strength increases as pH increases~ Bases decrease the number of hydrogen ions in solution

buffers

chemical system that maintains the pH if its an acid or base is added by removing H ions or adding H ions


BLOOD IS EX.

pH scale

~ 0-6: Acids- Going down the line from 6-0, hydrogen increases while hydroxide decreases~ 7: H20~ 8-14: Bases- Going up the line from 8-14, hydrogen decreases while hydroxide increases

major macromolecules

carbohydrates: monosaccharide


lipids: glycerol + fatty acid


proteins: amino acid


nucleic acids: nucleotide

carbohydrates

CHO


1:2:1 ratio



CARBOHYDRATES:


monosaccharides

6 carbons- hexose


5 carbons- pentose


glucose - photosynthesis, fuel for cellular respiration, "blood sugar"


fructose - sweet sugar


ribose - part of nucleic acid structure

isomer

same formula, different structure

CARBOHYDRATES:


disaccharides

double sugars


releases a water molecule


glucose + fructose = sucrose + h2O


glucose + glucose = maltose + h2O

COndensation reaction

two molecules join and a water molecule is released

lingkage between monosaccharide units

glycosidic lingkage

hydrolysis

large molecule splits into two subunits, water is needed

CARBOHYDRATE:


Polysaccharride

huge macromolecule


2 Functions: energy storage & structure

CARB - POLY: Starch

plants; used for energy storage


insoluble in water


2 types: amylose & amylopectin

CARB - POLY: Cellulose

plants; used for structure - cell wall


most abundant organic substance on earth

CARB - POLY: Gylcogen

animals; energy storage; stored in livers

Lipids

CHO


divided into:


fats, oils, waxes


phospholipids


steroids

why are lipids excellent energy storage compounds?

2x the energy as carbs per gram

5 functions 4 lipids

-insulation


- absorbtion


- protection


- structure of cell membrane


- hormones

why eating carbohydrates cause fat storage

carbohydrate is converted to fat

LIPIDS - Fats, Oils, and Waxes: during break down of triglyceride what reactant is needed?

H2O


hydrolysis



LIPIDS - Fats, Oils, and Waxes: Plant fats

unstaurated


liquid


corn oil


bent molecule


easy to breakdown

LIPIDS - Fats, Oils, and Waxes: animal fats

staurated


solid


butter


straight


hard to breakdown

PROTEINS

macomolecules w/ specific 3D shape


CH,O,N + S

Functions of proteins

- enzyme - catalysts rgulate metabolism


- structure - hair, membrane


- messengers - hormones


- transport - carry material in body


- antibody - defends body


- energy - food reserves

PROTEINS: are made up of, how many types (#), found in..?

amino acids


20


DNA

PROTEINS: two amino acids form?

dipeptide




peptide bond

PROTEINS: CLASSIFIED as

- fibrous proteins: stringy, insoluble


- Globular proteins: blobby, soluble

macromolecules

polymers made of monomers

monomers

linked togethers by condensation reaction


seperated by hydrolysis

amino acid R-groups

- polar


- nonpolar


- electrically charged - acidic or basic

R-groups can affect

solubility


position of proteins in membrane


forming channels through membrane


forming specific active sites in enzymes

PROTEIN STRUCTURE: Primary

unique sequence of amino acids

PROTEIN STRUCTURE: Secondary

btn peptide bonds


coils and folds in a polypeptide caused by hydrogen bonds btn hydrogen and oxygen atoms near the peptide bond


USUALLY TAKES FORM OF:


alpha or beta

PROTEIN STRUCTURE: Tertiary Structure

btn R-groups


supercoiling of a polypeptide stabilized by side-chain interations including covalent bonds,

PROTEIN STRUCTURE:TERTIARY - disulfide bridges

covalent bonds btn cysteine residues in a polypeptide that stabilizes tertiary structure

PROTEIN STRUCTURE:Quaternary

more than one tertiary structure to complete a protein

LAWS OF THERMODYNAMICS

-states that energy cannot be created or destroyed in a chemical reaction


- in all energy exchanges, if no energy enters or leaves the system, the potential energy of the state will always be less than that of the initial state


- entropy of a system approaches a constant value as the temperature approaches absolute zero

LAWS OF THERMODYNAMICS: entropy?

the measure of a system's thermal energy per unit temperature that is unavailable for doing useful work

ENZYMES: substrate?

the reactant that an enzyme acts on when it catalyzes a chemical reaction

ENZYMES: active site?

location where the substrate binds to an enzyme

ENZYMES: substrate enzyme complex?

an enzyme with its substrate attached to the activity site

ENZYMES:Induced fit model

sunbstrate binds to an enzyme


requires enzyme to "fit" into activity site


done by modifying substrate to fit in activity site

ENZYMES: define

an enzyme is a protein with a catalyctic function that speeds up the reaction. Many enzymes ... read quiz

ENZYMES: commercial uses

baking: modification of flour


brewing: chill-proofing


dairy: cheese


starch: soft drinks


leather: unhairing

Active transport

movement of material across the cell membrane against the concentration gradient and requires energy


forms: protein pumps, exocytosis, endocytosis= pinocytosis & phagocytosis

Passive transport

movement of material across the cell membrane with the concentration gradient and does not require energy


forms: diffusion, facilitated diffusion, osmosis

PASSIVE TRANSPORT: Diffusion

movement of form a high concentration to a low concentration


- particles bounce and collide randomly (brownian movement) until evenly dispersed


Rate of diffusion affected by:


temperature, pressure, and initial concentration

PASSIVE TRANSPORT: Osmosis

movement of water across a semi-permeable membrane with concentration gradient


Isotonic- same as cell


hypotonic- more in cell than outside


hypertonic- less in cell than outside

PASSIVE TRANSPORT:Facilitated

diffusion is aided by protein channels in membrane (integral proteins)

ACTIVE TRANSPORT: Exocytosis

exits out of cell

ACTIVE TRANSPORT: Endocytosis

Into the cell


Pinocytosis: liquids


Phagocytosis: solids

ACTIVE TRANSPORT: Protein pumps

cells unable to pass cell membrane due to non-polarity of fatty acid chains


INTEGRAL PROTEINS provide pathways


- energy is required