A&P Unit 1 - homeostasis, lipids, proteins

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55 Terms

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Anatomy
the study of form and structure of the body

\-WHAT is body part
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Physiology
the study of how organism functions

\-HOW and WHY it works
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Microscopic anatomy (2 subtypes)
can’t see with naked eye

\-cytology = study of cells

\-histology = study of tissues
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gross/macroscopic anatomy (5 subtypes)
can see with naked eye

\-systemic = of each body system

\-regional = focus on one area of body

\-surface = only on surfaces

\-comparative = compare across species

\-embryology = how develops from conception to birth
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types of physiology (5 types)
\*\*studying how and why these systems work

\-cardiovascular

\-neurophysiology

\-respiratory

\-reproductive

\-pathophysiology (disease)
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6 characteristics of living things
Organization

Metabolism

Growth

Responsiveness

Reproduction

Regulation

(OMGRRR)
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\-organization
complex structure and order of organism’s parts
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\-metabolism
organism uses nutrients

anabolism = build nutrients, use energy

catabolism = break nutrients, release energy
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\-growth & development
organism uses materials from environment to grow
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\-responsiveness
organism sense & react to environment stimuli
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\-reproduction
organism make new cells for growth & repair (mitosis) OR make sex cells (meiosis)
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\-regulation
organism ability to maintain homeostasis
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homeostasis
maintain consistent internal environm. even with external environm. changing
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interstitial fluid
fluid that fills space btwn cells
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internal v external environment
internal = interstitial fluid → temp, pH, etc

external = outside env. of organism (ex. my dorm)
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what are the ways of internal env. regulation?
conformity = ‘cold-blooded’ organism IE matches EXE

regulation = ‘warm-blooded’ organism maintain stable IE despite change in EXE
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What factors are homeostatically regulated?
\-nutrients/blood sugar → energy

\-O2 & CO2 → need for respiration & pH

\-concentration of waste products

\-electrolyte/water balance

\-pH → enzyme function

\-temp → cell & enzyme function

\-vol & (blood) pressure → for transportation
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what are the components of homeostatic systems?
1) RECEPTOR detects changes from the STIMULUS

2) CONTROL CENTER interprets & initiate change

→ nervous system = quicker response. endocrine = slower response

3) EFFECTOR is structure that brings changes
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negative feedback
move __toward__ homeostasis by minimizing impact of stimulus

Ex. shivering to stay warm in winter
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positive feedback
move __away from__ homeostasis by amplifying stimulus

→ until __climactic event__ occurs, then goes back to homeostasis

Ex. blood clot, childbirth, breastfeeding
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Individual response
individual organism alter own physiology in response to smth
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population/evolutionary response
change in gene pool over generations
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what are the types of individual response?
acute = short period (min-hours) change. modify existing cells

chronic = long period (days-month) change. restructure/build new parts
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acclimation
chronic response changes in __one__ way (usually in lab w/ controlled variables)
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acclimatization
chronic response changed in __many__ ways (happens naturally instead of in lab)
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hydrogen bond
__weak__ bond btwn H & O in water.

can form up to __4__ H bonds for 1 water molecule (2 from O and 1 each from H)
__weak__ bond btwn H & O in water.

can form up to __4__ H bonds for 1 water molecule (2 from O and 1 each from H)
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functions of water
\-body temp regulation

\-transportation

\-lubricant

\-spinal fluid

\-solvent for hydrophilic molecules
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solvent vs solute
solvent = dissolving agent

solute = gets dissolved

forms solution
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electrolytes
\-ionic compounds

\-completely dissolve

\-can conduct current

\-salts or acid/bases
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nonelectrolytes
\-polar compounds

\-dissolve in water but remain intact

\-can’t conduct current

\-ex. glucose
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water surrounds ions in a _____________
hydration shell
hydration shell
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hydrophobic exclusion & hydrophobic interaction
when water molecules “force out” nonpolar molecules → NP molecules need a protein carrier in the body
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amphipathic
partially dissolves in water. part P and part NP

ex. phospholipid
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functions of lipids
\-store energy

\-cell membrane components

\-make steroids
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what are the classes of lipids?
P.E.T.S.

Phospholipids

Eicosanoids

Triglycerides

Steroids
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fatty acid
chain of lipid made of C and H. nonpolar
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Triglyceride
\-most common lipid

\-hydrophobic, NP

\-1 glycerol + 3 fatty acid tail

\-created by joining glycerol via __lipogenesis__
\-most common lipid

\-hydrophobic, NP

\-1 glycerol + 3 fatty acid tail

\-created by joining glycerol via __lipogenesis__
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unsaturated, saturated, polyunsaturated triglyceride
unsat = no double bonds. solid @ room temp

sat = 1 double bond. liquid @ RT

polyunsat = 2+ double bond
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Phospholipid
\-cell membrane bilayer

\-amphipathic

\-polar phosphate group in head with 2 NP fatty acid tails
\-cell membrane bilayer

\-amphipathic

\-polar phosphate group in head with 2 NP fatty acid tails
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Steroid
\-nonpolar

\-4 carbon ring structure

\-side chains make them unique

\-ex. cholesterol, estrogen, testosterone, bile salts
\-nonpolar

\-4 carbon ring structure

\-side chains make them unique

\-ex. cholesterol, estrogen, testosterone, bile salts
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cholesterol
\-type of steroid

\-plasma membrane flexibility

\-precursor to other steroid synthesis
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Eicosanoids
\-20 carbon chain fatty acid

\-signal molecules

\-inflammatory response & nervous system communicators (think back to pain response in microbio)
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classes of eicosanoids
prostaglandin

prostacyclin

thromboxane

leukotriene
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a protein is _______
a __polymer__ made from __monomers__ of amino acids
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amino acid overview
\-1 amine group, 1 carboxyl group, side R chains

\-__20 types__ of amino acids

\-peptide bond created by __dehydration synthesis__
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lengths of peptides
oligopeptide = 3-20 AAs

polypeptide = 21-199 AAs

protein = 200+ AA’s
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four types of AAs
\-nonpolar

\-polar

\-charged

\-AAs with special function
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Nonpolar AAs
\-has only H-C bonds

\-group with other NP AAs → hydrophobic exclusion
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polar AA’s
\-R grp has more than H-C (usually O or N)

\-interact with water and other polar AAs
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charged AAs
\-R grp has +/- charge

\-forms ionic bond btwn other charged AAs

\-hydrophilic
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AAs with special function
\-proline - cause bend in protein chain

\-cysteine - can form disulfide bond

\-methionine - MET. start marker, first AA during protein synthesis
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1° Primary Structure
sequence of AA’s
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2° Secondary Structure
H-bonds → coiling of peptide chain

\-a-helix

\-b-pleated sheet
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3° Tertiary Structure
3D shape of protein as it folds→ affected by H-phobic or philic interactions of peptides

\-fibrous protein = skinnier and straighter. insoluble in water. structural support in body (ex. muscle)

\-globular protein = like a blob. soluble in water. chemical process/metabolism (ex. enzymes)
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4° Quaternary Structure
more folding. only appears if protein is made of 2+ polypeptides