Week 1 Molecular interactions Flashcards
Elements
Smallest form of matter, consisting of atoms
Atom contains
2 particles, protons (+) and neutrons (no charge)
What orbits the atom
electrons (-)
Neutral atom
equal number of electrons and protons
octet rule
outer most orbit has 8 electrons
chemical bond
Electrons experience a force attraction from both atoms & this (-/+/-) attraction holds the two atoms together
covalent bonds
when to atoms share electrons
Ionic bond
one atom gains electrons becoming an anion, and one loses an electron becoming a cation
Ions
Loos or gain of electrons causes atoms to gain a charge and now they are called IONS.
(cation/anion)
major ions in the body
Hydrogen, Carbon, Oxygen, Sodium, Potassium, Calcium, Phosphate & Chloride
molecular polarity
When electrons are unevenly distributed with in the molecule creating poles.
Polar molecules
One end has a (+) charge (pole), Other end has a (-) charge (pole)
nonpolar molecules
No charge on the molecule
hydrogen bonds
The (+) end of 1 molecule gets attracted to a (-) end of another molecule forming the Hydrogen bonds
Ranges of pH
0-14, (acidic:0-7, neutral:7-8, basic 8-14)
Acid
Donates H⁺ ions to a solution ( H₂CO₃ - Carbonic Acid)
Base
Binds with H⁺ ions from solution
HCO₃ - Bicarbonate
Buffer
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)
Buffer system found in our body: when pH is increased
Carbonic Acid Bicarbonate System- CO2H2O->H2CO3->H+HCO3
Buffer system found in our body: when pH is decreased
HCO3+H->H2CO3->CO2+H2O
decrease in pH means :
there is a lot of “H” in your blood so to get rid of it
Increase in pH means:
there is not enough “H” in your blood and you need to produce more
4 main classes of organic molecules
carbohydrates, lipids, proteins, nucleic acids
Carbohydrates
Monosaccharides, Disaccharides, Oligosaccharides, and polysaccharides
What are the three types of lipids
phospholipids, triglycerides, steroids
Saturated triglycerides
cause of cardiovascular disease
Unsaturated triglycerides
good fats, stored and serves as energy
phospholipids structure and function
Structure: head(hydrophilic) & Tail(hydrophobic) Function: Plasma membrane
Amino acids
building blocks for proteins, 20 types
out of 20 How many amino acids produced by your body
11
out of 20 how many amino acids produced by your diet
9
polypeptides
100 or more amino acids in a chain
what does homocysteine (AA) do if increased
Increase levels = increase chances of cardiovascular disease
Gama- Amino-Butyric Acid (AA) is a :
Neurotransmitter
Creatine (AA)
provides energy to muscles
codon
3 nucleotides
1 codon =
1 amino acid
Proteins are
fundamental components of all living cells
How are proteins produces
via two complex processes: transcription and translation
Primary structure of a protein
polypeptide/polypeptide chain (chain of amino acids)
Secondary structure of a protein
alpha helix(right handed spiral) or beta pleated sheet(2 polypeptides linked together)
tertiary structure of a protein
3D and functional
quaternary structure of protein
two or more of the tertiary structures put together
only ___ and ___ are functional structures. ___ and ___ are not.
only tertiary and quaternary are functional structures. Primary and secondary are not.
inactive proteins start with a __ or end with a ___.
inactive proteins start with a “pro” or end with a “ogen.”
Protein activity can be controlled, either by
activating it or inhibiting it.
Such factors are called Protein Modulators.
Activators: activate proteins
Proteolytic activators,
Allosteric activator, &
Cofactors (ions, small organic functional groups)
Inhibitors: Inhibit proteins
Competitive Inhibitor & Allosteric inhibitor (noncompetitive inhibitor)
allosteric activator
a modulator that binds to a protein away from binding site and turns it on
proteolytic activator
protein is inactive until peptide fragments are removed
cofactor
required for an active binding site, w/o cofactor protein is inactive
3 main cofactors in the body
(magnesium calcium iron)
Noncompetitive inhibitor(allosteric inhibitor)
a modulator that binds to a protein away from binding site and turns it off
competitive inhibitor
competes with Ligand for the binding site
The competitive inhibitor can be reversed if
you increase ligand concentration
protein denaturation
Permanent disruption of protein structure, leading to loss of function. Proteins revert back to primary structure from tertiary/quaternary
DNA is often called a
polynucleotide because they are made of nucleotides
Structure of DNA nucleotide
phosphate, sugar, and a base
Sugar in DNA
deoxyribose
Bases in DNA
adenine, guanine, cytosine, thymine
strands in DNA are linked via
hydrogen bonds
DNA backbone
phosphate/sugar
DNA interior
Bases
Nucleotide binding rule
Adenine - Thymine, Cytosine - Guanine
DNA characteristics
complimentary, hydrogen bonds sustaining helix formation, and antiparallel
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’
What does RNA stand for and what is its function
ribose nucleic acid, Function: protein synthesis
Types of RNA
mRNA(messenger), tRNA(transfer), rRNA(ribosomal)
which type of RNA can you find in the nucleus
only mRNA
which kind of RNA can you find in cytoplasm
all three, mRNA/tRNA/rRNA
RNA composition
sugar-ribose, phosphate and a base
Bases of RNA
adenine-uracil, guanine-cytosine
What does ATP stand for and what is it
adenosine triphosphate, energy molecule
What is NAD nucleotide and what is its function
nicotinamide adenine dinucleotide, it is a cofactor- carries INDIFFERENT form of energy
What is FAD and what is its function
flavin adenine dinucleotide, it is a cofactor- carries INDIFFERENT form of energy
What is cAMP and what is its function
cyclic adenine monoculceotide, signal transduction
