Bio Midterm

Front 1

amino acids

Back 1

basic structural units of proteins, consist of an amino group, a carboxyl group, an R group, and a hydrogen.

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polypeptides

Back 2

polymers of amino acids linked by peptide bonds (strong covalent bonds)

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primary structure

Back 3

the linear array of amino acids connected by peptide bonds (strong covalent bonds)

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secondary structure

Back 4

contains alpha helix and beta pleated sheets; formed by hydrogen bonds between polar- negative O on the carboxyl groups and polar-positive H of non-amino groups

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denaturation

Back 5

the process by which a protein loses its structure due to the disruption of polar bonds

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tertiary structure

Back 6

the 3-D structue of a polypeptide created by forming of covalent bonds, polar bonds, electrostatic attractions and non-polar repulsion among amino acids.

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quaternary structure

Back 7

a complex of several polypeptide chains linked together, more than on polymer

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structural protein

Back 8

provide support; ex. keratin, collagen, actin and myosin

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transport proteins

Back 9

carrier molecules such as albumin, hemoglobin, and cytochromes

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messenger proteins

Back 10

communicate one part of a body with another such as oxytocin, vasopressin, and insulin

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enzymes

Back 11

proteins that provide surfaces on which other molecules (substrates or ligands) gather and react.

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why is the egg white?

Back 12

proteins are denatured by acidity, baseity, and heat and the denatured proteins form lines that stack up ontop of each other which prevents light from passing through it making it white

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heat affects on proteins

Back 13

heat causes the molecules to vibrate which causes the hydrogen bonds to break.

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pepsin

Back 14

an enzyme that breaks down proteins into amino acids

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amylase

Back 15

an enzyme that breaks sown starch into monosaccharides Lab 4

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% transmittance

Back 16

percentage of light that passes through the substance in the cuvette of a spectrophotometer

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% absorbance

Back 17

% of light that does not pass through the substance in a spectrophotometer

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cold temps on proteins

Back 18

cause the enzyme to slow way down and it does not break down very much of the starch very fast

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nuclein

Back 19

DNA discovered by Meicher from pus

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EDTA

Back 20

a chelating agent that binds metallic ions like MG++ which acts as a cofactor for DNase

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micelles

Back 21

formed in the cloudy liquid and is extracted by chloroform

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ice cold ethanol

Back 22

used to precipitate DNA

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diffusion

Back 23

movement of particles to equilibrium throughout

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strong acid

Back 24

dissociates into many H+ ions

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strong base

Back 25

dissociates into many OH- ions

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osmosis

Back 26

the passive movement (by simple diffusion) of water molecules across a selectively permeable membrane

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physiological saline

Back 27

isostonic solution used in the elodea cell slide preparation to act as the control

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1.0 M NaCl

Back 28

solution used in elodea cell slide preparation to act as the hypertonic slide

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distilled water on slide

Back 29

used in elodea cell slide preparation to serve as the hypotonic solution

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lower molarity leads to....

Back 30

greater rate of osmosis

Front 31

equation to find slope of egg mass change vs. molarity

Back 31

E(XY)-E(X)E(Y)/n
______________
E(X2)-E(X2)/n

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to find b or y intercept

Back 32

plug in sum of x for x and sum of y for y and the slope and solve for b

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if the molarity concentration is smaller,

Back 33

then the change in the mass of the egg will be greater due to increased osmolarity

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egg exercise (lab 5)

Back 34

the eggs were originally soaked in acetic acid to dissolved the shell. then the eggs were placed in varying molarities of either sucrose or NaCl. The eggs were weighed before and again after they sat in the solution for an hour. Measurements taken to the .1 g.

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lab 5

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egg mass change vs. molarity; Elodea cell slide exercise; then found equations for the egg part

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elodea cell isotonic

Back 36

lots of green but also white spaces

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elodea cell hypertonic

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the cell plasma has shrunk because water has moved out of the cell; little green dots and lots of white;1.0 M NaCl

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elodea cell hypotonic

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distilled water; the cell plasma is swelled and is completely green

Front 39

cuvettes

Back 39

test tube like with a vertical and horizontal white lines on it; used to calibrate the spectrophotometer

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spectrophotometer

Back 40

used to find the quatitative value of how the enzymes were affected; also used to show how much light passes through a solution and how much is absorbed

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phosphate group in DNA

Back 41

makes DNA a polar molecule

Front 42

5' and 3' end of DNA

Back 42

5' end has the phosphate group on it and the 3' end has the hydroxyl group attached to it

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periodic acid

Back 43

used to convert the complex carbohyrates into aldehydes by breaking the bond between the one and two carbons which makes them into monosaccarides and then turns them into aldehydes for the shiff reagant to stain

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shiffs reagent

Back 44

stains aldehydes; used to show the presence of polysaccharides

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hematoxylin

Back 45

stains DNA and therefore the nucleus; which allows us to differentiate the nucleus from the presence of polysaccharides

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benedicts reagant and heat

Back 46

used to find the presence of glucose or simple sugars with the presence of a colored precipitate

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benedicts reagant, heat, and HCl

Back 47

used to test for the presence of sucrose with a colored precipitate; the acid and heat breaks the polysaccharides into monosaccharides and then the benedicts reacts with the monosaccharides

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iodine

Back 48

used to indicate the presence of iodine with a dark blue color

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if there are carbohydrates around or in the cytoplasm,

Back 49

then we expect the presence of a dark pink stain to show their location

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type 1 error

Back 50

when one rejects the null hypothesis

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type (II) error

Back 51

when on rejects the alternative error

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lab 4

Back 52

enzyme sensitivity using the spectrophotometer, DNA in onion isolation

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lab 3

Back 53

identifying unkown carbs using iodine, benedicts, and HCL; PAS reaction with slide showing presence of polysaccharides

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diatase

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enzyme that digests starch and glycogen so that the aldehyde functional groups cannot form

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central dogma

Back 55

refers to a series of processes where genomic information is used to make the necessary proteins for biological activities

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bright field microscopy

Back 56

uses a series of glass lenses to bend light waves and create a magnified image

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SEM/TEM

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creates the magnified images by using electrons instead of light waves; show 3-D images at a higher magnification than light waves

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fluorescent microscopy

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uses a mcuh higher intesity light source, which excites a fluroescent species in a sample of interest. The species in turn emits a lower energy light of a longer wavelegth that produces the magnified image instead of the original light source

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agranulocytes

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devoid of granules and include monocytes and lymphocytes

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granulocytes

Back 60

also know as polymorphonuclear leukocytes contain visible granules, segmented nuclei and include basophil, neutrophil, and eosinophil.

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red blood cells

Back 61

most abundant, sacrifice and eject their nucleus when they are adults so they can contain more hemoglobin and carry oxygen

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platelets

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tiny fragments of cells; used to clot blood

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white blood cell

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only cell that has a nucleus

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1 ocular space =

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(# hashmarks of stage)(value of stage)
___________________________
(#Hashmarks on ocular)

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oil immersion

Back 65

a technique used to increase the resolution when using a 100x objective; oil has the same refractive properties as glass so it decreases light scattering because it focuses more light from the specimen into the 100x objective

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most important part of the microscope

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good resloution

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lab 2

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cross fibers depth of field; oil immersion; artifacts vs. specimen' calibration of micrometer; identifying white blood cells and chi square test

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compund microscope

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uses two or more objectives to achieve a higher magnification

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ocular

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eyepiece

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total magnification

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multiply the objective by the ocular objective to get total

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condenser

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focuses light on specimen

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iris diaphragm

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changes the intensity of the light

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parfocal

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when the microscope remains in focus when magnification is changed

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working distance

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the distance between the objective lens to the specimen

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field of view

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the amount of specimen that can be seen at one time

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depth of field

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the thickness of the specimen that can be seen in focus at one time

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substances used in second diffusion experiment

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copper, potassium permanganate, potassium dichromate; and methylene blue

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agar

Back 78

a kind of gelatin used in lab one second diffusion experiment, it is a kind of gelatin made from refined seaweed and water, 1g of agar for every 100 ml of water making it a 1% agar solution.

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diffusion rate

Back 79

length traveled/time

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ranking of most diffusion

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potassium permanganate, potassium dichromate, methylene blue, copper

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if the molecular mass is high

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then the rate of diffusion will be slow only when they are soluble

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diffusion

Back 82

all particles have kinetic energy so the bounce around until they are all evened out and in equilibrium

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NH4OH

Back 83

base used in first diffusion reaction, the precipitate was closer to this end

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HCL

Back 84

acid used in first diffusion reaction, farther from this end due to small molecular mass than the NH4OH

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Brownian movement

Back 85

random movement of particles suspended in a gas or liquid and the atoms are in perpetual motion as long as the temp surrounding them is above absolute zero, O K, -273.15 C, -459.67 F

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accuracy

Back 86

describes the nearness of a measurement to the theoretical value

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precision

Back 87

describes the degree to which several measurements provide answers very close to each other

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K

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C+273.15

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C

Back 89

K-273

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F

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9/5 C +32

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C

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5/9 F - 32

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coplin jars

Back 92

have ridges or shelves for slides to be placed in, used for the PAS experiment