Anatomy And Physiology: Ch. 2

Front 1

biochemistry

Back 1

study of chemical composition and reactions of living matter

Front 2

organic compounds

Back 2

-contain carbon
-covalently bonded molecules
-many large
-includes proteins, carbs, lipids (fats), nucleic acids

Front 3

inorganic compounds

Back 3

-don't contain carbon
-include water, salts, acids, bases

Front 4

water

Back 4

-most abundant inorganic compound
60%-80% of volume

Front 5

water properties

Back 5

1) high heat capacity
2) high heat of vaporization
3) polar solvent properties
4) reactivity
5) cushioning

Front 6

water: high heat capacity

Back 6

-absorbs & release large amounts of heat
-prevents changes in temp. (homeostasis)- water redistributes heat

Front 7

water: high heat of vaporization

Back 7

-changes form liquid to gas
-heat absorbed breaks H bonds
-sweat- heat removed from body providing cooling mechanism

Front 8

water: polar solvent properties

Back 8

water- universal solvent
polarity- water molec. moves from neg. ends toward pos. ends
-explains how compounds dissociate
-forms hydration layers

Front 9

water as an excellent solvent

Back 9

nutrients, resp. gases, metabolic wastes carried throughout body- dissolved in blood plasma & metabolic wastes excreted from urine

Front 10

water: reactivity

Back 10

-most important reactant
hydrolysis- add water to break bond
dehydration- water molec. is removed to form bond

Front 11

water: cushioning

Back 11

-form resilient cushion around certain body organs
-helps protect from physical trauma

Front 12

salts

Back 12

-ionic compound containing cations other than H+ and anions other than hydrodxyl ion OH-
-inorganic, dissolves in water
-expl: NaCl, CaCo3, KCl

Front 13

electrolytes

Back 13

substances that conduct electrical current

Front 14

acids

Back 14

-have sour taste
-react w/ metals, burn "hole"
-release hydrogen ions (H+)
-proton donors
-concent. of H+ determines acidity

Front 15

bases

Back 15

-have bitter taste
-feel slippery
-release hydroxyl ions (OH-) & take up H+
-proton acceptors
expl: bicarbonate ion (HCO3-)
ammonia (NH3)

Front 16

pH: Acid-Base Concentration

Back 16

-based on concentration of hydrogen ions
-more H+, more acidic
-more OH-, more basic
runs from 0-14
pH: 7.00 neutral
pH: 0-6.99 acidic
pH 7.01-14 basic

Front 17

neutralization

Back 17

-joins H+ or OH- to form water and neutralizes solution
-acids & bases mixed, forms water and salt

Front 18

buffers

Back 18

-resist abrupt and large swings in pH of body fluids

Front 19

strong acids

Back 19

-dissociate completely & irreversibly in water
-can dramatically change pH

Front 20

weak acids

Back 20

don't dissociate completely

Front 21

strong base

Back 21

dissociate easily in water & quickly join with H+

Front 22

weak base

Back 22

ionizes incompletely and reversibly
expl: bicarbonate ion

Front 23

carbonic acid-bicarbonate system

Back 23

-carbonic acid dissociates reversibly
-release bicarbonate ions & protons
-chem. equilibrium between carbonic acid (weak acid) & bicarbonate ion (weak base) resists changes in blood pH

Front 24

carbon is electroneutral

Back 24

-never loses or gains electrons
-always shares electrons

Front 25

carbohydrates

Back 25

-group of molecules that includes sugars and starches
contain C, H, O
classified according to size/solubility

Front 26

monosaccharides

Back 26

structural units or building blocks of carbohydrates

Front 27

monosaccharides

Back 27

-simple sugars
-single-chain or single-ring structures
-contain 3 to 7 carbon atoms
-C, H, O

Front 28

disaccharides

Back 28

-double sugars
-two monosaccharides joined by dehydration synthesis
expl: glucose+fructose=sucrose
glucose+galactose=lactose
glucose+glucose=maltose

Front 29

polysaccharides

Back 29

-long chains of simple sugar
-linked by dehydration synthesis
-units: polymers
-expl: starch and glycogen (glucose)

Front 30

starch

Back 30

-storage carbs formed by plants
-must be digested to be absorbed

Front 31

glycogen

Back 31

-storage carbs of animal tissues
-sorted in skeletal muscle & liver cells
-highly branched & large molec.

Front 32

carbohydrate function

Back 32

-source of cellular fuel
-dietary carbs convert to glycogen or stored fat

Front 33

lipids

Back 33

-insoluble in water
-dissolve readily in other lipids
-contain C, H, O
-have lower portion of O than carbs
-types: triglycerides, phospholipids, steroids

Front 34

triglycerides

Back 34

-are neutral fats
-composed of fatty acids and glycerol
-fatty acids: linear chains of C, H
-glycerol: modified simple sugar
-nonpolar molec: don't interact w/ water
-efficient & compact form of stored energy
-found beneath skin

Front 35

saturated fats

Back 35

-one single covalent bonds between carbon atoms
-fatty acid chains are straight & packed closely together to form solid

Front 36

unsaturated fats

Back 36

-contain one or more double bonds between carbon atoms
-cause fatty acid chains to kink
-more healthy
-can't be packed closely to solidify
-expl: olive/peanut oils

Front 37

trans fats

Back 37

-include margarines & baked products
-oils solidified by addition of H atoms to double carbon atoms
-increases heart disease

Front 38

phospholipids

Back 38

-modified triglycerides
-phosphorous-containing group and two fatty acid chains
tail-nonpolar head-polar

Front 39

steroids

Back 39

-flat molec. made of four interlocking hydrocarbon rings
-fat soluble and contain little oxygen
-expl: cholesterol

Front 40

eicosanoids

Back 40

-diverse lipids derived from a 20-carbon fatty acid
-expl: prostaglandins- roles in blood clotting, inflammation, & labor contractions

Front 41

proteins

Back 41

-contain C,H,O,N and many contain sulfur and phosphorus
-expl: enzymes, hemoglobin of blood, and contractile proteins of muscle

Front 42

amino acids

Back 42

-are building blocks of proteins
-20 common amino acids
-have amine & organic acid group

Front 43

peptide bond

Back 43

-bond that links the amino acids
-joined by dehydration synthesis

Front 44

primary structure

Back 44

-linear sequence of amino acids composing polypeptide chain
-structure is the backbone of protein molecule

Front 45

secondary structure

Back 45

- twists & bends
-common type: alpha (α)-helix (coils)
beta (β)-pleated sheet-don't coil, linked side by side by hydrogen bonds to form pleated, ribbonlike structure

Front 46

tertiary structure

Back 46

α-helical or β-pleated regions of polypeptide chain fold upon one another to produce compact ball-like, or globular molecule

Front 47

quaternary structure

Back 47

-two or more polypeptide chains for complex protein
exp: hemoglobin

Front 48

fibrous proteins

Back 48

-extended and strandlike
-called structural protein
-exhibit only secondary structure, some quaternary
-expl: collagen, keratin, elastin
-insoluble in water and very stable
-provide mechanical support and tensile strength

Front 49

collagen

Back 49

-most abundant protein in body
-part of fibrous protein

Front 50

globular proteins

Back 50

-compact, spherical proteins
-have tertiary structure, some exhibit quaternary
-water soluble, chemically active molecules, and play roles in all biological processes
-called functional proteins

Front 51

protein denaturation

Back 51

-hydrogen bonds break when pH drops or temp. rises
-causes proteins to unfold & lose specific 3-dimen. shape
-can no longer perform roles

Front 52

active sites

Back 52

Region on surface of (globular) protein where it binds/interacts chemically with other molec.

Front 53

molecular chaperones or chaperonins

Back 53

-help proteins to achieve functional three-dimensional structure
-ensures folding is quick & accurate

Front 54

enzymes

Back 54

-globular proteins that act as biological catalysts
-chemically specific

Front 55

catalysts

Back 55

-substances that regulate & accelerate rate of biochem. rxn
-increase speed of reaction

Front 56

the body utilizes this type of organic molecule first for energy when needed

Back 56

carbohydrate

Front 57

the type of bond that links amino acids together

Back 57

peptide bond

Front 58

this compound forms a bilayer in the cell plasma membrane

Back 58

phospholipids

Front 59

the storage form of glucose in the body

Back 59

glycogen

Front 60

a classification for fats that contain double bonds and prevent them from freezing

Back 60

unsaturated fats

Front 61

the concentration of this element in a solution determines the pH

Back 61

hydrogen

Front 62

the term applied to a protein that has lost its 3-dimensional shape

Back 62

denatured

Front 63

this type of compound resists abrupt & excessive changes in the pH of a solution

Back 63

buffers

Front 64

this chemical process uses water to break apart a bond

Back 64

hydrolysis

Front 65

proteins are classified by shape & configuration. Hemoglobin is classified as a _______type of protein.

Back 65

quaternary