Midterm exam for HLTH 2110

Units 1,2,3,4,5

Anatomy

Study of structure

Physiology

Study of function in organisms

Structure-function relationship example

Gas exchange, extremely thin alveoli helps more easily remove CO2 waste from blood and O into blood

Levels of Organization and examples

Atom: Oxygen, Molecule: Dioxide, Macromolecule: phospholipid, cell: clara cell, tissue: epithelial, organ: lung, organ system: respiratory system, organism: human body

Thoracic cavity subdivisions

pleural (lung) cavity, mediastinum

Negative feeback loop example

Water balance, body temp high and low

Positive feedback loop example

childbirth

Photon sources

Nuclear rearrangement, nuclear fission, electron rearrangement

How many protons do hydrogen, carbon, nitrogen and oxygen have?

Hydrogen: 1, Carbon: 6, Nitrogen: 7, Oxygen: 8

When number of neutrons changes the atom is called an

isotope

Isotopes of Hydrogen

Protium, Deuterium, Tritium; Protium is most common, Tritium is radioactive and unstable

Isotopes of Carbon

12C, 13C, 14C; carbon 12 most common

Radioisotope names

Alpha decay, Beta decay, positron emission

Alpha particles are

Helium nuclei, with 2 protons and 2 neutrons

Beta particles are

electrons with negative charge

Positrons are

antimatter electrons, same mass but opposite charge

Atomic number is

amount of protons

mass number is

protons+neutrons

Periodic Table F

Fluorine

Endothermic vs Exothermic

Endothermic absorbs energy, exothermic releases energy

Ionic bonds

Large difference in electronegativity

Acids

donate a hydrogen ion

Bases

accepts a hydrogen ion

-OH

Hydroxyl group

-NH2

Amino group

-HCO3

Bicarbonate ion

pH is measured on a

logarithmic scale

buffer

minimizes pH changes

Most important buffer system in human biology

Carbonic acid- bicarbonate buffer system

Colloid

a solution where particles are able to scatter light

Molarity

Concentration of substance within specific volume

Avogadro’s number

6.02 × 10²³

Osmolarity

number of dissolved particles in a solution

hypertonic

water out of cell, shrinsk

Isotonic

perfect balance of water going in and out of cell

Hypotonic

Too much water into cell, bursts

-OH

Hydroxyl

-SH

Sulfhydrul

-NH2

Amino

R1-CH2-R2

Methylene

R-CH3

Methyl

C6H6 R-C6H5

Phenyl (benzene ring)

OⅡR1–C–O–R2

OⅡR1–C–O–R2

Ester

R–COOH

Carboxyl

OⅡR–C–H

Aldehyde

R1–C–O–C–R2

Ether

CH3-COOH

Acetic Acid (methyl+carboxyl)

OⅡR1–C–R2

Ketone

Acidic functional groups

Carboxyl, -COOH and -COO-

Basic functional groups

Sodium bicarbonate: NaHCO3, Bicarbonate ion: HCO3-, Amino: -NH2, Amino (charged): -NH3+

CH3COO-

Acetate (methyl and carboxyl), polyatomic anion

HCO3-

Bicarbonate, polyatomic anion

CO3²-

Carbonate, polyatomic anion

H2PO4-

Dihydrogen phosphate, polyatomic anion

OH-

Hydroxide, polyatomic anion

HPO4²-

Monohydrogen phosphate, polyatomic anion

NO3-

Nitrate, polyatomic anion

NO2-

Nitrite, polyatomic anion

O2²-

Peroxide, polyatomic anion

PO4³-

Phosphate, polyatomic anion

SO4²-

Sulfate, polyatomic anion

NH4+

Ammonium, polyatomic cation

H3O+

Hydronium, polyatomic cation

Ethanol and glycerol

alcohols

In benzene rings chemicals are polar or nonpolar?

nonpolar, if it all share the same

Protein monomers and polymers

Monomers: amino acids, Polymers: polypeptides

Carbohydrate monomers and polymers

Monomers: Monosaccharides (glucose fructose and galactose), polymers: Cellulose, starch and glycogen

Lipids monomers and polymers

Monomers: fatty acids, Polymers: triglycerides

Nucleic acids monomers and polymers

Monomers: nucleotides, polymers: RNA, DNA

Amino acids have what groups

Amino (NH2) group and Carboxylic acid (-COOH) group

Amino acids are chained together by a covalent bond called a

peptide bond

Peptide bonds are formed by

dehydration synthesis

Negatively charged R groups

Aspartate, glutamate and methylene

Positively charged amino acids

Lysine, Arginine, Histidine

Nonpolar, aliphatic R groups

Proline, methionine, isoleucine, leucine, glycine, alanine, valine

Nonpolar aromatic R gropus

Phenylalanine, tyrosine, tryptophan

Polar uncharged R gropus

Cysteine, serine, threonine, asparagine, glutamine

Primary sequence of a protein is

order in which amino acids are connected

a Helix protein structure

secondary structure, hydrogen bonded and spiral structure

B pleated sheet

Secondary structure, pleated sheet, hydrogen bonds

Interactions that keep proteins folded

Ionic bonds, hydrophobic interactions, disulfide linkages, hydrogen bonds

Protein motif

Commonly seen arrangements of proteins that serve specific purpose

Most enzymes are named by adding the suffix

-ase onto the name of the substrate (e.g. oxidases, transferase, hydrolases, lyases, isomerases, ligases)

Enzymes do what to the activation energy of chemical reactions

lowers the activation energy

cofactor/coenzyme

substance that improves efficiency of enzymes as catalysts

Purine nitrogenous bases

adenine and guanine

Nitrogenous base + sugar

nucleoside

Neucleotide parts

sugar, phosphate, nitrogenous base

Our cells read and assemble RNA and DNA in what direction

5’-3’

Denaturation is the process of

changing the shape

What makes up ATP

Adenine, ribose and phosphates

Where does energy come from in an ATP molecule?

When the bonds between phosphates are broken and release stored energy

Plasma membrane looks like a

bilayer sheet

Glycolipids and glycoproteins are both used for

cell to cell recognition

Monomers of lipids are called

fatty acids

Steroids are within the …. group. The backbone of all steroids is a …. molecule.

lipid, cholesterol

How many double bonds between carbons does a saturated fatty acid have?

0

Fatty acids are made up of a … end and a … end.

lipid, acid

A polyunsaturated fatty acid has at least … double bonds between ….. which causes a …. in the molecule.

2, carbons, kink

The formation of a triglyceride comes about through dehydration synthesis. What molecules are combined in this process?

3 fatty acids and 1 glycerol