AP 1 Lecture Exam 1

posterior (dorsal) aspect

contains cavities encased in bone, subdivided into 2 cavities: cranial cavity and vertebral canal

fate of pyruvate

depends on oxygen availability

enough O2: pyruvate enters mitochondria

low O2: pyruvate converted to lactate

product of glycolysis

product of intermediate stage

pyruvate

Acetyl CoA

ventral cavity

anterior aspect split by thoracic diaphragm into superior thoracic cavity and inferior abdominopelvic cavity

appendicular

upper and lower limbs

axial

along the central axis of the body, consists of: skull, vertebral column, sternum, and ribs

thoracic cavity

contains mediastinum, plueral cavity, and pericardial cavity

abdominopelvic cavity

contains abdominal cavity and pelvic cavity

abdominopelvic regions

umbilical, epigastric, right/left hypochondriac, hypogastric, right/left lumbar. right/left iliac

homeostasis

an organisms ability to maintain consistent internal environment in response to external conditions

the 4 part system of homeostasis

stimulus, receptor, control center, effector

negative feedback

resulting reaction will always be opposite direction of the stimulus, activate biological processes to return conditions to set point

ex: pancreas relasing insulin when bloode glucose increases above set point

positive feedback

increase variable in same direction until climactic event occurs then body returns to homeostasis

ex: breastfeeding, baby suckles and stimulates breast to eject breast milk

abdominopelvic quadrants

right/left upper, right/left lower

pericardium:

what are the outer and inner layers called

what is the cavity called inbetween layers called

what fluid does it contain

2-layered serous membrane that encloses heart

(outer) parietal pericardium and (inner) visceral pericardium

pericardial cavity

contains serous fluid

metabolism:

what processes does it consist of

sum of all chemical reactions within the body

anabolism and catabolism

anabolism

building up or synthesizing, increased size (growth) and increased specialization related to form and function (development)

catabolism

breaking down or decomposition, this happens to get nutrients body needs

homeostatic imbalance

disease

covalent bonds

within a molecular compound it is formed between 2 or more atoms by sharing electrons, occurs when both atoms require electrons

ex: CO2, H2O

ionic bonds

cations and anions bound by electrostatic interactions, a.k.a salts

ex: NaCl, MgCl2

characteristics of a radioisotope

when an element has an unbalanced ratio of protons to neutrons in its nucleus, unstable form of an element, experience radioactive decay relesing excess energy in the form of electromagnetic waves or particles

structure of an atom

3 forms of matter

solid, liquid, gas

ion

atoms with a positive (cation) or negative charge (anion), produced from loss or gain of one or more electrons

cation

positive charge

ex: Na+, H+

anion

negative charge

ex: Cl-, HCO3-

atomic number

number of protons in an atom of the element, above symbol name, number of electrons is same as number of protons

atomic mass number

mass of protons and neutrons, neutron number = atomic mass - atomic number [(p+n)-p]

phospholipids: structure

amphipathic molecules, gycerol with a phosphate group (hydrophilic: polar) head and fatty acid (hydrophobic: nonpolar) tails

phospholipids: function

serves as chemical barriers for cell membranes

ampipathic

chemical or molecule that posses both polar and nonpolar properties

functions of liquid water

transports, lubricates, cushions, and excretes wastes

what is pH

measure of the relative amounts of H+ (hydrogen ions) a neutral, acidic, or basic solution has, number between 0 (very acidic) and 14 (very basic/alkaline)

optimal range of pH for enzymes

6-8, or 7.45

acid

dissociates in water to produce H+ and an anion, it is a proton donor, which increases concentration of free H+, more dissociation of H+ with strong acids, less dissociation with weaker acids

base

decreases concentration of free H+, more absorption of H+ with stronger bases, less absorption with weaker bases

what is a protein structure

what kind of bonds link them together

one or more strands of amino acid monomers

linked by peptide bonds

4 types of protein structures

primary, secondary, tertiary, and quaternary

primary structure

linear sequence of amino acids

secondary structure

patterns that repeat several times

2 types: alpha helix (spiral coil), beta sheet (planar sheet arrangement)

tertiary structure

3d shape of a poly-peptide chain

2 types: globular proteins (fold into compact shape), fibrous proteins (extended linear molecules)

quaternary structure

present in proteins with 2 or more polypeptide chains

ex: hemoglobin

types of lipids

triglycerides, phospholipids, steroids, eicosanoids

triglycerides: function and structure

long term energy storage, formed by glycerol and 3 fatty acids

3 types fatty acids

each type has how many double bonds

saturated: lacks double bonds, unsaturated: one double bond, polyunsaturated: 2 or more double bonds

steroids: function and structure

composed of hydrocarbons, regulate growth, development, and reproduction

eicosanoids: function and structure

local signaling molecules, inflammatory response and nervous system communication, modified 20-Carbon fatty acids

4 classes of eicosanoids

prostaglandins, prostacyclins, thromboxanes, and leuotrienes

nucleic acids: function

what are the 2 classes

store and transfer genetic information

deoxyribonucleic acid (DNA) and ribonucleic acid (RNA)

DNA and RNA are polymers composed of waht type of monomers

what covalent bond links them

nucleotide

phophodiester bonds

what are the nucleotide monomers made up of

sugar: 5-Carbon pentose, phosphate group, and nitrogenous base

what are carbohydrates (CH2O)n

what are the 3 types of carbohydrates

body’s primary source of fuel

monosaccharides (glucose, fructose, ribose, deoxyribose) = 1, disaccharides (sucrose, lactose, maltose) = 2, polysaccharides = 3 or more

kinetic energy

energy of motion

glucose

glycogen

provides energy to cells

many glucose molecules

potential energy

energy of position or stored energy

phosphodiester bonds

strong covalent bond that links 2 sugars and a phosphate group

what is ATP composed of

nitrogenous base adenine, ribose sugar, and 3 phosphate groups

what is ATP

nucleotide, it is the central molecule in transfer of chemical energy within a cell

descibe an amino acid

organic compounds that combine to form proteins

structural formula

indicates the arrangement of atoms within a molecule

molecular formula

indicates the number of atoms

endergonic reactions

synthesis, reactants with less energy than products, energy supplied, net increase in potential energy

exergonic reactions

decomposition, reactants with more energy than products, energy released, net decrease in potential energy

redox reactions (oxidation-reduction)

exchange reaction where electrons are moved from one chamical structure to another, ionic bonding is redox, redox reactions always occur together

thermodynamics

study of heat transfer

1st and 2nd laws of thermodynamics

energy can neither be created or destroyed it can only change form

when energy is transformed some energy is lost to heat

enzymes

biolgically active catalysts that accelerate chemical reactions, decrease activation energy of cellular reactions

activation energy

energy required to break existing chemical bonds (determines the reaction rate) activation energy barrier must be overcome to start reaction

what does induced fit create

a highly stable enzyme-substrate complex and an optimal transition state that accerletaes chemical reactions

enzyme-substrate complex

temporary molecular structure formed when a substrate molecule binds to the active site of an enzyme

what suffix is associated with enzymes

-ase

optimal pH for enzymes

6-8

what feedback mechanism that enzymes are regulated by

negative feedback

phosphorylation

addition of a phosphate group

enzyme that carries out phosphorylation

kinase or phosphorylases

dephosphorylation

what is the enzyme that carries this out

removal of phosphate group

phosphatases

what is the common way that ATP is produced

aerobic cellular respiration

cellular respiration steps

glycolysis, intermediate stage, citric acid cycle, electron transport chain

what is another name for cellular respiration

glucose oxidation

what are the products of cellular respiration

ATP (30 net, 38 gross), water and carbon dioxide

what are the products of citric acid cycle for 2 turns

2 ATP, 6 NADH, 2 FADH2

what happens at rest with muscle tissue

uses steady supply of oxygen to break down fatty acids instead of glucose

irreversible reaction

net loss of reactants and net gain in products

reversible reaction

reaction moves in both ways, no net change in concentration of either reactants or products (equilibrium)