Chapter 2: Anatomy and Physiology Marieb - Anthony Morgan St

matter

anything that occupies space and mass

energy

the capacity to do work

kinetic energy

energy in action

potential energy

stored energy that has potential to do work but is not doing so

Name and define four types of energy and give examples of where they can be found in the body

chemical energy (breaking or forming of chemical bonds, e.g. digestion to create ATP); electrical (movement of charged particles e.g. nervous system uses nerve impulses); mechanical (energy involved in moving matter e.g. moving muscles to run); electromagnetic (wave energy e.g. x-rays and ultraviolet rays to make vitamin D)

Energy conversions

Not very efficient, and a lot of supply lost as heat. ex. lightbulbs emit light and heat

elements

substances that can't be broken down into simpler substances

4 elements prevalent in body

CHON

atoms

Building blocks of matter

atomic symbol

first letter(s) of elements name ex. Ca stands for calcium

Protons

Positive charge subatomic particle (1 amu)

neutrons

neutrally charged subatomic particles (1 amu)

electrons

negatively charged subatomic particles (0 amu)

Why are atoms electrically neutral?

Same number of protons and electrons

orbitals

regions around nucleus in which electrons are to be found most of the time

atomic number

number of protons in nucleus

mass number

masses of the protons and neutrons

isotopes

same number of protons but different number of neutrons

atomic weight

average of all relative abundance mass numbers of all isotopes / number of isotopes

radioisotopes

isotopes that are unstable that decompose into stable forms, used in cancer research to localize and illuminate damaged tissue

molecules

combination of two atoms of the same element held together by chemical bond

compound

two or more different kinds of atoms binding e.g. H2O

Mixtures

PHYSICALLY INTERMIXED not chemically intermixed unlike compounds

solutions

homogenous mixtures of components, substance present in largest amount is solvent (dissolving medium), smaller amount is solute, naturally transparent and don't scatter life

What is the units of a solution

percent (parts per hundred percent) or milligrams per deciliter, or molarity (moles per liter indicated by M)

mole

molecular weight (sum of atomic weights) weighed out in grams

colloids

heterogenous mixtures, solute particles are larger. cytosol is a colloid

suspensions

heterogenous mixture with large solutes that settle out. blood is a suspension

valence shell

outermost shell of atom with electrons

octet rule

atoms react by gaining or losing electrons so as to acquire the stable electron structure of a noble gas, usually eight valence electrons

ionic bond

atoms formed by transfer of one or more electrons. Atom that gains one or more electron is the electron acceptor (anion negative charge), and atom that loses electrons is the electron donor (cation and has positive charge)

Describe ionic bond NaCl

Na has one electron in valence, Cl has 7 electrons in valence. Na is the electron donor and gives electron to Cl, and Cl is electron acceptor. most ionic compounds are salts.

Covalent bonds

shared electrons produce molecules that occupy single orbital common to both atoms. single covalent bond is when two atoms share one pair of electrons. some atoms share two or three electron pairs and these are double and triple covalent bonds

Polar vs non polar-covalent bond

unequal sharing of electrons (slight negative change at one end of molecule, slight positive charge at other end-- dipole) vs equal sharing of electrons (charge balanced among atoms)

electronegative vs electopositive

electronegative hog electrons and gain them due to valence shell with 6,7 electrons, and electropositive tend to lose valence shell electrons

hydrogen bonds

attractions rather than two bonds, ex. oxygen from one H2O attracts hydrogen from another so they cling together forming surface tension

chemical reaction

when bonds are formed, rearranged, broken

chemical equation

reactants --> products in equilibrium

synthesis reaction

anabolic activities such as joining small molecules into large protein molecules

decomposition reaction

broken down into smaller molecules (catabolic)

exchange or displacement reactions (give example)

both synthesis and decomposition e.g. ATP to ADP reaction; redox reaction. reactant losing electrons is the electron donor and is oxidized. reactant taking up electrons is electron acceptor and is reduced.

exergonic reactions

A chemical reaction associated with the release of energy to the surroundings, oxidative and exergonic

endergonic reactions

chemical reactions that require energy, typically anabolic

chemical equilibrium

In a chemical reaction, the state in which the rate of the forward reaction equals the rate of the reverse reaction, so that the relative concentrations of the reactants and products do not change with time.

What influences the rate of chemical rxns

temperature (higher faster), concentration (higher faster), particle size (smaller faster), presence of catalysts e.g. enzymes

biochemistry

study of chemical composition and reactions of living matter

organic compounds characteristics

contain carbon, covalently bonded, large

inorganic

water, salts, acids, bases

Why is water so useful to life

high heat capacity (low resistance to temperature changes), high heat of vaporization (efficient cooling while sweating), universal solvent, it is important reactant in body with respect to hydrolysis (add water to break bond) and dehydration synthesis (remove water to make bond), and cushioning around organs

salts

ionic compounds containing cations other than H+ and OH-. they dissociate in water and conduct electricity. electrolytes help with nerve impulse and muscle contratction

acids

releases hydrogen ions and is just a hydrogen nucleus, called proton donors because they release hydrogen ions and anions.

e.g HCl--> Cl- + H+

bases

proton acceptors and they take up hydrogen ions. They dissociate to form hydroxyl ions and cations.

e.g. NaOH --> OH- + Na+ and OH- + H+ -> H2O . bicarbonate ion and ammonia (waste product) are found in body

pH units

more hydrogen ions more acidic, more hydroxyl ions more basic. 7 is neutral.

strong acids

strong acids: dissociate irreversibly and completely in water and dramatically change the pH

Buffer

They resist changes in pH by releasing H+ ions when pH increases and binding H+ when pH decreases. Homeostasis of acid base balance is regulated by kidneys and lungs by buffers. Weak acid and conjugate base or weak base and conjugate acid.

weak acids

weak acids: partial dissociation, only some dissociate fully into ions and others don't. e.g. acetic acid

100 HAc--> 90 HAc + 10 Ac- + 10 H+ ; also HAc ⇌ Ac- + H+

When you add H+ to the acetic acid solution, some of ti combines with Ac- and goes to HAc. When you add strong base, equilibrium shifts to teh right and more HAc molecules dissociate to release H+

It's a buffer system.

strong base

hydroxides dissociate easily in water and tie up H+, like hydroxides

What happens when acids and bases are mixed?

react in displacement to form water and salt. It neutralizes the solution.

weak base

ionizes incompletely and reversibly and accept only a few protons

carbonic acid-bicarbonate system

H2CO3 ⇌ HCO3- + H+

weak acid weak base proton

When pH rises, the rxn shifts right and carbonic acid dissociates and releases protons, when pH lowers, rxn shifts left and as bicarbonate ions bond with protons

exceptions to generalization of organic compounds

Carbon dioxide and carbon monoxide are considered inorganic compounds

electroneutral

carbon never loses or gains electrons, only shares them, can join long rings in the body

polymers

chainlike molecules made up of units called monomers which are joined in dehydration synthesis

carbohydrates

sugars and starches that contain CHON, larger the carbohydrate molecule the less soluble

monosaccharide and give examples

simple sugar, single chain, single ring structure. pentose (deoxyribose) and hexose (glucose, galactose, fructose) sugars are examples of monosaccharides

isomers

same molecular formula, different arrangements of atoms. galactose and fructose are isomers of glucose

disaccharide and give example

double sugar formed from two monosaccharides from dehydration synthesis, can't move through membranes so they break apart by hydrolysis (sucrose, lactose, maltose)

sucrose = which two monosaccharides

lactose = which two monosaccharides

maltose = which two monosaccharides

glucose + fructose

glucose + galactose

glucose + glucose

polysaccharides and give examples

large polymers of simple sugar, fairly insoluble. Starch is storage carbohydrate and cellulose is a polysaccharide. in animals it is glycogen (storage for animals in muscle and liver cells)

functions of carbohydrates

energy storage that is ready and useable

Properties of lipids and name three main types

insoluble in water. types include triglycerides, phospholipids, steroids. don't have much oxygen in comparison

Another name for triglycerides

Neutral fats

triglyceride

fats when solid, oil when liquid. Made up of fatty acids and glycerol in 3:1 ratio. MOST efficient and compact form of stored energy. found mainly beneath skin and insulate from heat loss, and protect from trauma. can be saturated or unsaturated

fatty acids make up?

Fatty acids are linear chains of hydrocarbons and an organic acid group (-COOH) at one end.

glycerol make up?

glycerol is a modified simple sugar (sugar alcohol)

How are triglycerides made?

dehydration synthesis to attach fatty acid chains to glycerol

Properties of saturated fatty acids

solid at room temperature. single covalent bonds only, and completely straight. mostly found in animal fats.

Properties and types of unsaturated fatty acids

2 types, mono and polyunsaturated). Double covalent bonds between carbon atoms that cause them to kin, remain liquid at room temperature. found in plants.

Trans fats

oils that have been solidified by addition of H atoms at sites of carbon double bonds. Increase risk of heart disease.

Phospholipids make up and where you can find in body

phosphorous containing group called the polar head + glycerol back bone + 2 fatty acid chains. hydrocarbon portion is nonpolar tail, and phosphorous containing head is polar and attracts water and ions. it is used in cell membranes (e.g. phospholipid bilayer)

Steroid make up and where to find them in body

flat molecules of four interlocking hydrocarbon rings. fat soluble and contain little oxygen. example is cholesterol. found in cell membranes and vital to homeostasis.

Eicosanoids

diverse lipids from 20 carbon fatty acid chain. most important is prostaglandins which play roles in blood clotting, regulation of blood pressure, labor contractions etc

Proteins

structural material of body (e.g. keratin in skin and nails, muscles), enzymes, hemoglobin, insulin. contain CHNOPS (only proteins have nitrogen)

Amino acids and make up

building blocks of protein. Made up of amine group (NH2), a functional R group and organic acid group -COOH. They can act as either an acid (proton donor) or base (proton acceptor).

What makes amino acids chemically unique

differences in the R group

Peptide bond

Long changes of amino acids joined together by dehydration synthesis. Amine is linked to -COOH in the next. Two joined is dipeptide, 3 is tripeptide, 4+ is polypeptide, 50+ is a protein

macromolecules

most proteins are large and complex containing from 100 to 10,000 amino acids joined by peptide bonds in which amine is connected to carboxylic acid via dehydration synthesis

How many amino acids are there?

20. Using some combination of these, thousands of different types of proteins are constructed

Primary structure of protein

amino acid beads are the backbone of protein molecule

Secondary structure of proteins

Alpha helix (primary chain coiled to form spiral structure stabilized by hydrogen bonds). and beta sheets (primary chain zig zags forming pleated sheet and adjacent strands are held together by hydrogen bonds).

tertiary structure

A helical or B pleated sheets of the polypeptide chain fold to form a compact globular molecule. Structure maintained by both covalent and hydrogen bonding

Quaternary structure

two or more polypeptide chains with tertiary structure combine to form functional protein

Fibrous proteins and another name for them

also called structural proteins. extended and strand like. insoluble and stable. some secondary structure, and most have tertiary or even quaternary structure as well. collagen, keratin, elastin, and contractile proteins of muscle

globular proteins and another name for them

functional proteins. have at least tertiary structure. water soluble, chemically active and unstable. prone to denaturation. examples include antibodies for immunity, enzymes like amylase in saliva to breakdown starch, hemoglobin for oxygen transport in blood, albumin for regulation of pH, molecular chaperones to create new proteins and breakdown damaged ones

Factors causing denaturation

hydrogen bonds are fragile and can break easily due to low pH, high temperature and loses its shape and functionality

Denaturation

Can be restored, but if its too damaged then it can't be cured. For globular proteins, the active sites can be destroyed and they no longer work. if blood ph to acidic, hemoglobin will not be able to bind and transport oxygen.

molecular chaperones

Molecular chaperones aid folding of new proteins in both healthy and damaged cells and transport of metal ions into and within the cell. They also promote breakdown of damaged protein. ex. stress proteins produced in variety of traumatizing stimuli and can patch up damaged proteins and refold them

Enzymes

biological catalysts that accelerate rate of biochemical reactions but are not used up. they lower the activation energy (energy amount required to break bonds of reactant) required for a reaction.

two parts of enzyme, what is it called? what are the two parts.

collective is called holoenzyme. there is apoenzyme (protein portion) and cofactor (metal ion like copper or iron) /coenzyme (usually vitamins)

substrate

substance on which an enzyme acts