Week 1 Molecular interactions Flashcards

1
Q

Elements

A

Smallest form of matter, consisting of atoms

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2
Q

Atom contains

A

2 particles, protons (+) and neutrons (no charge)

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3
Q

What orbits the atom

A

electrons (-)

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4
Q

Neutral atom

A

equal number of electrons and protons

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5
Q

octet rule

A

outer most orbit has 8 electrons

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6
Q

chemical bond

A

Electrons experience a force attraction from both atoms & this (-/+/-) attraction holds the two atoms together

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7
Q

covalent bonds

A

when to atoms share electrons

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8
Q

Ionic bond

A

one atom gains electrons becoming an anion, and one loses an electron becoming a cation

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9
Q

Ions

A

Loos or gain of electrons causes atoms to gain a charge and now they are called IONS.
(cation/anion)

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10
Q

major ions in the body

A

Hydrogen, Carbon, Oxygen, Sodium, Potassium, Calcium, Phosphate & Chloride

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11
Q

molecular polarity

A

When electrons are unevenly distributed with in the molecule creating poles.

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12
Q

Polar molecules

A

One end has a (+) charge (pole), Other end has a (-) charge (pole)

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13
Q

nonpolar molecules

A

No charge on the molecule

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14
Q

hydrogen bonds

A

The (+) end of 1 molecule gets attracted to a (-) end of another molecule forming the Hydrogen bonds

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15
Q

Ranges of pH

A

0-14, (acidic:0-7, neutral:7-8, basic 8-14)

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16
Q

Acid

A

Donates H⁺ ions to a solution ( H₂CO₃ - Carbonic Acid)

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17
Q

Base

A

Binds with H⁺ ions from solution

HCO₃ - Bicarbonate

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18
Q

Buffer

A

A substance that minimizes pH change of that solution when a “acid/base” is added to it (tries to keep the pH as close to the same as possible)

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19
Q

Buffer system found in our body: when pH is increased

A

Carbonic Acid Bicarbonate System- CO2H2O->H2CO3->H+HCO3

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20
Q

Buffer system found in our body: when pH is decreased

A

HCO3+H->H2CO3->CO2+H2O

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21
Q

decrease in pH means :

A

there is a lot of “H” in your blood so to get rid of it

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22
Q

Increase in pH means:

A

there is not enough “H” in your blood and you need to produce more

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23
Q

4 main classes of organic molecules

A

carbohydrates, lipids, proteins, nucleic acids

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24
Q

Carbohydrates

A

Monosaccharides, Disaccharides, Oligosaccharides, and polysaccharides

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25
What are the three types of lipids
phospholipids, triglycerides, steroids
26
Saturated triglycerides
cause of cardiovascular disease
27
Unsaturated triglycerides
good fats, stored and serves as energy
28
phospholipids structure and function
Structure: head(hydrophilic) & Tail(hydrophobic) Function: Plasma membrane
29
Amino acids
building blocks for proteins, 20 types
30
out of 20 How many amino acids produced by your body
11
31
out of 20 how many amino acids produced by your diet
9
32
polypeptides
100 or more amino acids in a chain
33
what does homocysteine (AA) do if increased
Increase levels = increase chances of cardiovascular disease
34
Gama- Amino-Butyric Acid (AA) is a :
Neurotransmitter
35
Creatine (AA)
provides energy to muscles
36
codon
3 nucleotides
37
1 codon =
1 amino acid
38
Proteins are
fundamental components of all living cells
39
How are proteins produces
via two complex processes: transcription and translation
40
Primary structure of a protein
polypeptide/polypeptide chain (chain of amino acids)
41
Secondary structure of a protein
alpha helix(right handed spiral) or beta pleated sheet(2 polypeptides linked together)
42
tertiary structure of a protein
3D and functional
43
quaternary structure of protein
two or more of the tertiary structures put together
44
only ___ and ___ are functional structures. ___ and ___ are not.
only tertiary and quaternary are functional structures. Primary and secondary are not.
45
inactive proteins start with a __ or end with a ___.
inactive proteins start with a "pro" or end with a "ogen."
46
Protein activity can be controlled, either by
activating it or inhibiting it. | Such factors are called Protein Modulators.
47
Activators: activate proteins
Proteolytic activators, Allosteric activator, & Cofactors (ions, small organic functional groups)
48
Inhibitors: Inhibit proteins
``` Competitive Inhibitor & Allosteric inhibitor (noncompetitive inhibitor) ```
49
allosteric activator
a modulator that binds to a protein away from binding site and turns it on
50
proteolytic activator
protein is inactive until peptide fragments are removed
51
cofactor
required for an active binding site, w/o cofactor protein is inactive
52
3 main cofactors in the body
(magnesium calcium iron)
53
Noncompetitive inhibitor(allosteric inhibitor)
a modulator that binds to a protein away from binding site and turns it off
54
competitive inhibitor
competes with Ligand for the binding site
55
The competitive inhibitor can be reversed if
you increase ligand concentration
56
protein denaturation
Permanent disruption of protein structure, leading to loss of function. Proteins revert back to primary structure from tertiary/quaternary
57
DNA is often called a
polynucleotide because they are made of nucleotides
58
Structure of DNA nucleotide
phosphate, sugar, and a base
59
Sugar in DNA
deoxyribose
60
Bases in DNA
adenine, guanine, cytosine, thymine
61
strands in DNA are linked via
hydrogen bonds
62
DNA backbone
phosphate/sugar
63
DNA interior
Bases
64
Nucleotide binding rule
Adenine - Thymine, Cytosine - Guanine
65
DNA characteristics
complimentary, hydrogen bonds sustaining helix formation, and antiparallel
66
antiparallel
applied to two molecules that are side by side but run in opposite directions, one strands runs: 5’ – 3’ and the other strand runs: 3’ – 5’
67
What does RNA stand for and what is its function
ribose nucleic acid, Function: protein synthesis
68
Types of RNA
mRNA(messenger), tRNA(transfer), rRNA(ribosomal)
69
which type of RNA can you find in the nucleus
only mRNA
70
which kind of RNA can you find in cytoplasm
all three, mRNA/tRNA/rRNA
71
RNA composition
sugar-ribose, phosphate and a base
72
Bases of RNA
adenine-uracil, guanine-cytosine
73
What does ATP stand for and what is it
adenosine triphosphate, energy molecule
74
What is NAD nucleotide and what is its function
nicotinamide adenine dinucleotide, it is a cofactor- carries INDIFFERENT form of energy
75
What is FAD and what is its function
flavin adenine dinucleotide, it is a cofactor- carries INDIFFERENT form of energy
76
What is cAMP and what is its function
cyclic adenine monoculceotide, signal transduction