Cter 2: Chemical Level Of Organization Flashcards

1
Q

What are the most common major elements?

A

Oxygen (most common), carbon, hydrogen, nitrogen

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2
Q

Significance of oxygen

A

Part of h2o, many organic molecules, used to generate atp, temporarily store chemical energy

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3
Q

Significance of carbon

A

Backbone of chains and rings in all organic molecules: carbohydrates, lipids, proteins, nucleus acids

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4
Q

Significance of hydrogen

A

Water, most organic molecules, makes bodily fluids more acidic

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5
Q

Significance of nitrogen

A

Component of all proteins and nucleic acids

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6
Q

Significance of calcium

A

Provides structure , blood clotting

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7
Q

What forms chemical bonds, stores energy in bonds, and exists in orbitals

A

Electrons

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8
Q

How to find atomic number

A

Number of protons in the nucleus of an atom
Number of protons = number of electrons

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9
Q

How to find mass number

A

Number of protons + number of neutrons in an atom

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10
Q

How to find atomic weight/mass

A

Weighted average of all naturally occurring isotopes

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11
Q

Isotope definition

A

Same number of protons and electrons but a different number of neutrons. Different mass number

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12
Q

Are radioisotopes more or less stable than isotopes

A

More unstable and decay to more stable isotope forms by releasing energy

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13
Q

Ion definition

A

Atom has lost if gained electrons to become more stable

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14
Q

Cation

A

Positively charged ion. Ion loses electrons. Na+

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15
Q

Anion

A

Negatively charges ion. Atom gains electrons. Cl-

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16
Q

Free radical

A

Atom or atoms with unpaired electrons in outermost shell. Can damage tissues

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17
Q

Common ions: bicarbonate ion

A

HCO3 -

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18
Q

Common ions: sulfate

A

SO4 2-

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19
Q

Common ions: phosphate

A

PO4 3-

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20
Q

Common ions: ammonium

A

NH4 +

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21
Q

Common ions: magnesium

A

Mg2+

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22
Q

Molecule definition

A

2+ atoms sharing electrons. O2

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23
Q

Compound definition

A

A substance that can be broken down into 2+ different elements. C6H12O6

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24
Q

When is an atom stable

A

When the outermost shell is full

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25
Ionic bond
Cation and anion. Electrons transferred from one atom to the next
26
Covalent bond
Atoms share electrons. Bonds are polar (bonds shared equally) and non polar (bonds shared unequally)
27
Hydrogen bonds
Attraction if oppositely charged polar molecules or parts of molecules. Very weak. Surface tension of water.
28
How to break hydrogen bonds. Change the shape of a protein.
Change in temp or pH
29
Reversible reaction
Products can revert back to original reactants
30
Oxidation reduction reaction
Transfer of electrons between atoms and molecules.
31
Activation energy
Energy required for a chemical reaction to occur. Enzymes act as a catalyst for rxn and decreases amount of energy needed to start a rxn
32
Biochemistry definition
Study if chemical composition and reactions of living matter
33
Which one of the major elements is not typically in inorganic compounds
Carbon. Except CO2, CO
34
Hydrophilic
Water soluble. Likes water
35
Hydrophobic
Water insoluble. Dislikes water.
36
Dehydration synthesis rxn
Water removed to make bonds. Monomers joined by removal of OH from one monomer and H from other at site of bond
37
Hydrolysis rxn
Water added to break bonds. Add OH to one monomer and H to other
38
Give an example of water as a lubricant
Joints, serous membranes
39
Electrolytes
Release ions in water and conduct electricity
40
Acids
Release hydrogen ions (H+) in water proton donor
41
Bases
Release ions (OH-) that can combine with hydrogen ions. Proton acceptor
42
Salts
Electrolytes that dissociate in water that aren’t H+ or OH-
43
Neutral pH
7
44
Acidic pH
<7
45
Basic
pH >7
46
Buffers
Help maintain homeostasis by converting strong acids/bases into weak acids/bases
47
Hydroxyl
OH-
48
Sulfhydryl
-SH
49
Carboxylic acid
-COOH
50
Ester
O=C-O
51
Amino
-NH
52
Carbohydrates
C, H, O. Hydrogen and oxygen in 2:1 ratio. Quickest source of energy. Monosaccharides, disaccharides, polysaccharides
53
Lipids
C, H, O. Sometimes P. Hydrophobic. Energy storage, insulation, protection.
54
Saturated fatty acids
Single covalent bonds. Tightly packed linear molecukes
55
Unsaturated fatty acids
Double bonds. Kink or bend so can’t pack close together.
56
Phospholipid
Head is polar and hydrophilic, tail is non polar and hydrophobic. Cell membrane structure
57
Steroids
Four interlocking ring structures. Cholesterol.
58
Proteins
C, H, O, N. sometimes P, S. polymers of amino acid monomers held by peptide bonds. Four structural levels
59
Amino acid bonds
Joined by covalent bonds called peptide bonds
60
Primary structure of proteins
Polypeptide chain. Amino acid sequence
61
Secondary structure protein
Beta pleated sheet. Twisting and folding of neighboring amino acids, stabilized by hydrogen bonds
62
Tertiary structure
Alpha helix. Three dimensional shape of polypeptide chain
63
Quaternary structure protein
Arrangement of two or more polypeptide chains
64
Enzymes
Globular proteins that act as biological catalysts. Specific, efficient, regulated by cellular controls
65
How do enzymes bind
Lock and key. Substrate binds to the active site of the enzyme. Enzyme catalyzes the reaction and turns subtrate into products. After rxn enzyme is unchanged
66
Nucleic acids
Made of C, H, O, N,and P held together by hydrogen bonds
67
DNA
genetic blueprint for all the synthesis of all proteins. Double stranded helix in cells nucleus
68
RNA
links DNA to protein synthesis. Single strand mostly outside of nucleus
69
3 types of RNA
mRNA, tRNA, rRNA
70
ATP
Chemical energy released when glucose is broken down. RNA nucleotide with two extra phosphate groups