bio midterm 1 (Purple Pages)

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Last updated 5:31 PM on 10/16/23
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121 Terms

1
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science is to

know

2
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investigative approach to acquiring knowledge by making observations about the natural world, developing explanations and testing those explanations

scientific method

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a hypothesis has to be

testable and falsifiable

4
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A failure to falsify a hypothesis does not...

prove that hypothesis

5
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compares an experimental group with a control group

controlled experiment

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remains constant

controlled variable

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scientifically acceptable and well-substantiated explanation of some part of the natural world, takes many years to establish, supported by exhaustive experimentation, and unlikely to be contradicted later

Scientific Theory

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when is observational science used

when its too difficult to establish controlled experiments

9
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basic unit of life

cell

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has mass and occupies space, consists of pure elements

matter

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a substance that cannot be broken down to other substances by chemical rxs

element

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a substance consisting of 2 or more elements in a fixed ratio

compound

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Which elements make up 96% of the matter in living organisms?

Hydrogen, Oxygen, Nitrogen, Carbon

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What makes living organisms so different?

Different proportion of elements, and the organizations of the molecules

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number of protons

atomic number

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protons and neutrons

atomic mass

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atoms with the same number of protons but different number of neutrons

isotopes

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isotopes have the same atomic number but

different atomic mass

19
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unstable isotopes that decay and release energy

radioisotopes

20
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rate of decay in an isotope is

constant

21
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the amount of time for it to break down, leaving half

half life

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a substance containing radioisotopes that is used to measure the speed of a chemical processes and/or movement of speed

radioactive tracers

23
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Why was there a global radioisotope shortage between 2007-2010?

Shut down of Chalk river in Canada, Produces 30-40% of world supply

24
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the number of electrons is equal to the number of

protons

25
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electron are in

orbitals

26
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Valence electrons determine an atom's

reactivity

27
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4 main types of chemical bonds

a. Ionic

b. Covalent

c. Hydrogen

d. van der Waals Forces

28
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transfer of electron from one atom to another

ionic (intra)

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sharing of a pair of valence electrons (have a distinct 3D form)

covalent bond (intra)

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structure is related to

function

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measure of an atom's attraction for electrons in a covalent bond

electronegativity

32
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unequal sharing of electrons

polar covalent bond

33
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Partial positive charge of H atom are attracted to partial negative charge of nearby atoms, weaker than covalent and ionic bonds

Hydrogen bonding (intermolecular)

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•Weaker than hydrogen bonds

•Develop between nonpolar molecules

•Constant motion of electrons causes them to accumulate by chance on one region of molecule

van der Waals forces (inter)

35
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water is more dense than

ice

36
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the structure of water gives it a ______ and allows for _________

high specific hear capacity , attraction between water molecules (cohesion)

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•Water molecules surround polar molecules and ions, allows for separation of molecules

Hydration Shell

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proton donor

acid

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proton acceptor

base

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•Controls pH by absorbing or releasing H+

• Most are weak acids or weak bases

Buffers

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What controls the pH of our blood?

Carbonic acid

42
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Living matter are all composed of carbon compounds

organic

43
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How many covalent bonds can carbon form?

4, this tetravalence makes large complex molecules possible

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•Vary in length and shape

• molecules where carbon is bound only to hydrogen

hydrocarbons

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single carbon bond

-ane

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double carbon bond

ene

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triple carbon bond

-yne

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•- reactive groups

- enter into biological reactions

- bind to carbon

functional groups

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1.(-OH)

hydroxyl

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2.(-C=O)

Carbonyl

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3.(-COOH)

Carboxyl

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4.(-NH2)

Animo

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5.(-PO42-)

Phosphate

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6. (-SH)

Sulfhydryl

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dehydration (remove water to form a bond)

synthesis of a polymer

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-hydrolysis reaction (add water to break a bond)

breakdown of a polymer

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Sugars and the polymers of sugars (fuel and building material)

Carbohydrates

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•Multiples of CH2O (1:2:1) (a-glucose easier for animal cells to breakdown)

monosaccharides

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Isomers of Monosaccharides have the same chemical formula, but different

molecular structure and function

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Enantiomers

isomers that are mirror images of each other

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difference between an aldehyde and a ketone

Different position of carbonyl group

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Covalent bond in between Disaccharides

glycosidic linkage

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2 glucose

maltose

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glucose and fructose

sucrose

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glucose and galactose

lactose

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amylose (alpha 1-4) is

unbranched

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glycogen is

branched

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has a beta 1-4 linkage with H-bonds

Cellulose

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has beta linkages and N-groups

chitin

70
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protein functions

- Structural support

- Storage

- Transport

- Enzymes in reactions

- Cellular communications

- Movement

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How many different human proteins?

over 100 000

72
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polymers amino acids

polypeptides

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How many different types of amino acids?

20

74
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carbon in a protein is called a

alpha protein

75
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Alanine (Ala, A)

Nonpolar

76
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Valine (Val, V)

nonpolar

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Leucine ( Leu, L)

nonpolar

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Isoleucine (Ile, I)

nonpolar

79
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Glycine (Gly, G)

nonpolar

80
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cystine (Cys, C)

Nonpolar, can b polar under a certain pH

81
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Phenylalanine (Phe, F)

Nonpolar

82
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Tryptophan, Trp, W

nonpolar

83
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Methionine, Met, M

nonpolar

84
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Proline, Pro, P

nonpolar

85
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Serine, Ser, S

polar, uncharged

86
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Threonine, Thr, T

polar, uncharged

87
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Tyrosine, Tyr, Y

polar, uncharged

88
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Asparagine, Asn, N

polar, uncharged

89
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Glutamine, Gln, Q

polar, uncharged

90
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Aspartic acid, Asp, D

negatively charged polar

91
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Glutamic acid, Glu, E

negatively charged polar

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Lysine, Lys, K

Polar basic, positive charge

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Arginine, Arg, R

Polar basic, positive charge

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Histidine, His, H

Polar basic, positive charge

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•Covalent bond

•Dehydration

•Amino acid added only to carboxyl end

peptides

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what kind of bonds do proteins have

peptide bonds

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linear sequence of amino acids

primary structure

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•H-bonds between amino acids

•O and H of backbone

folds into

-Alpha helix

-Beta pleated sheets

secondary structure

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•All types of bonds between R groups

form a 3D shape and Function

tertiary structure

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•≥ 2 polypeptides

•All types of bonds

Quaternary structure