Quiz 1 - Water, Acid/Base, Lipids, Nucleic acids, Peptides, Proteins Flashcards
Ionic bonding
Transferred electrons, can be strongest bonding
Covalent
Shared electrons, medium strength
Metallic
Electron cloud, least strong
Ion-dipole interaction
Dipole attracted to ion
H-bond
H covalently bonded to O, F or N interacts with other O, F or N
Dipole-dipole interaction
Dipoles interact with one another
Ion-induced dipole
Electronegativity of an ion generates a dipole in an otherwise inert molecule
Dipole-induced dipole
Electronegativity of a dipole generates a dipole in an otherwise inert molecule
Dispersion/van der Waals forces
Random movement of electrons produces a transient dipole
Water structure
H2O, 104.5 degree angle between H, dipole. Water has high specific heat because of H bonds
Ice
H2O forms ordered crystal lattice due to uniform angles and H bonds. Ice is less dense than liquid water and therefore floats
Amphipathic Molecules
Molecules that contain both a nonpolar and polar region
Water as a solvent
Water will spontaneously dissolve other molecules because of nonrandom arrangement involving dipole interactions
Lipids in water
Will form miceles or bilayers
Solutes in water
Effect colligative properties, raise BP, lower FP
Cell in Isotonic solution
Solute concentrations equal in intracellular and extracellular environment
Cell in Hypertonic solution
Solute in cell less concentrated than outside of cell, water leaves cell
Cell in Hypotonic solution
Solute in cell more concentrated than outside of cell, water enters cell
Proton hopping
Protons will hop around among water molecules
Keq
Equilibrium constant. = [Products]/[Reactants]
Kw
Water Keq. = 1X10^-14
pH scale
-log{H+]
pKa
Equilibrium constant of an acid
pH of an acid solution
pH = pKa + log [HA]/[A]
Buffer solutions
Weak acids will donate or accept electrons to maintain a consistent pH. Ex.) Bicarbonate H2CO3 HCO-
Respiratory Acidosis
CO2 retention from hypoventilation, decreases plasma pH
Respiratory Alkalosis
CO2 excretion from hyperventilation, increases plasma pH
Metabolic Acidosis
Increase of acidic molecules or decrease of basic molecules in plasma, decreases plasma pH
Metabolic Alkalosis
Decrease of acidic molecules or increase of basic molecules in plasma, increases plasma pH
Fatty Acid/Lipid functions
Store energy, form membranes, carry info/signals, additional services (vitamins, enzyme cofactors, colorants)
Fatty Acid
Carboxylic acid with long hydrocarbon chain
Saturated
No double bonds
Unsaturated
One double bond. Cis configuration most common in bio systems
Polyunsaturated
Multiple double bonds
Fatty acid nomenclature
C:#Unsats. Omega nomenclature numbers from end of HC chain to first unsat.
Fatty Acid Properties
More Carbons = Higher melting point, More unsats = Lower melting point
Lipid
One or more fatty acid connected to a linker molecule
Triglycerides
Storage lipids, 3 fatty acids attached to a glycerol
Phospholipids
One or two fatty acids attached to a glycerol or sphingosine with a Phosphate group attached, form membranes
Glycolipids
One or two fatty acids attached to a glycerol or sphingosine with a sugar group attached, function as anchors for proteins to membranes and as cell ID
Sphingolipids
Membrane lipids, one sphingosine, one fatty acid, involved in direct signaling activity
Sterols
Like Cholesterol. Major membrane components that increase membrane rigidity, necessary for endocytosis. Can be used as cell signals/hormones
Lipids and inflammation
Lipids drive and resolve inflammation. Aspirin and Tylenol are COX 1 & 2 inhibitors that prevent formation of proinflammatory signals from lipids. Fatty acid signals may help in preventing/curing periodontal inflammatory disease
Nucleotide
Pentose ring, purine or pyramidine base, 1-3 phosphates
Nucleoside
Same as nucleotide but with no phosphates
Nucleic acid
Nucleotides connected by phosphodiester bonds
Functions of nucleotides
- Information Transfer: DNA, RNA
- Energy Transfer: ATP, GTP, NADH
- Signal Transduction: cAMP, cGMP
Purines
Adenine and Guanine, dual cyclic
Pyramidines
Cytosine, Thymine, Uracil, one ring
DNA
Deoxyribonucleotide polymer, one OH on pentose ring, 2 stranded, contains thymine, only in nucleus
RNA
Ribonucleotide polymer, 2 OH on pentose ring, can be one stranded, contains uracil, found throughout cell, more reactive than DNA
Primary structure
Strand of nucleotides linked by phospho-diester bonds
Secondary structure
Pair of antiparalell strands
Tertiary structure
Double helix
Quaternary structure
Helix wrapped around histones to form chromosomes
Palindrome
Flipped mirror sequence
Mirror Repeat
Mirrored sequence on same strand
Double Helix Forms
A form, B form, Z form. A form each twist is 36 Angstroms
mRNA
DNA transcript that codes for protein production
tRNA
RNA molecule that tethers amino acids for translation
rRNA
RNA that forms Ribosomes
Regulatory RNA
aRNA, shRNA, siRNA, regulates translation, transcription, signaling
Nonessential Amino Acids
Alanine, Asparagine, Aspartate, Glutamate, Serine
Conditionally Essential Amino Acids
Arginine, Cysteine, Glutamine, Glycine, Proline, Tyrosine
Essential Amino Acids
Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine
Glucogenic Amino Acids
Used for gluconeogenesis. All but proline, leucine, and lysine
Ketogenic Amino Acids
Isoleucine, Leucine, Lysine, Phenylalanine, Tryptophan, Tyrosine
Stereoisomerism
Chiral centers, L and D conformations. L is most common in nature, Glycine is the only non-chiral amino acid.
Disulfide Bonds
Formed between two cysteines
Uncommon amino acids
4-Hydroxyproline and 5 hydroxylysine, components of collagen
Modifications of amino acids
Phosphorylation, Methylation, acetylation, adenylylation. Modify protein structure
Amino acids in bad breath
Ornithine, Citrulline
Zwitterion form
Net charge of 0 but 2 ions. NH3+ and COO-. Intermediate form between to buffering zones
How do amino acids form polymers?
Peptide bonds, N terminal to C terminal, via condensation (removal of H2O)
Levels of protein structure
Primary - sequence of amino acids
Secondary - helixes and B-sheets
Tertiary - Folds of folds
Quaternary - multiple subunits
Sickle-Cell Anemia
Single substitution of an amino acid in hemoglobin protein leads to malformed RBCs
Collagen Synthesis
Proteins synthesized > Procollagen strands > Tropocollagen > Collagen molecules > Fibril > Fiber
Where are plasma proteins produced?
Liver, except for immunoglobulins which are produced elsewhere
Denaturation
pH and high temperature cause Proteins to lose the H bonds, etc. that hold their structure