Bio/Biochem Flashcards
Chirality of AAs
All AAs are chiral (L) except glycine and they all are S except cysteine.
Nonpolar, nonaromatic AAs
glycine, alanine, valine, leucine, isoleucine, methionine, proline
Aromatic AAs
Tyrosine, tryptophan, pheynylalanine
Polar AAs
Serine, threonine, glutamine, asparagine, cysteine
Negatively Charged AAs
Glutamate and aspartate
Positively Charged AAs
Lysine, arginine, histadine
pI determination of AAs
Average of pKa values for each H of the AA
Peptide bond formation/breakdown
Condensation (dehydration) reaction to form with nucleophilic amino group attacking electrophilic carbonyl; hydrolysis to break
Primary structure
The AA sequence
Secondary Structure
local structure stabilized by H-bonding; includes a helices and beta pleated sheets
Tertiary Structure
3D structure stabilized by hydrophobic interactions, acid base interactions (salt bridges), hydrogen bonding, and disulfide bonds
Quaternary structure
Interactions between subunits.
Denaturation
Caused by heating or solutes.
Structural Proteins
Fibrous; include collagen, elastin, keratin, tubulin, actin
Motor Proteins
Capable of force generation through conformational change; myosin, kynesin, dynein
Binding Proteins
Bind a specific substrate, either to sequester it in the body or hold its concentration at a steady state
Cell Adhesion Molecules (CAMs)
Bind cells to other cells or surfaces, include cadhedrins, integrins, and selectins
Antibodies (immunoglobulins Ig)
Target a specific antigen which may be a protein in the surface of a pathogen or a toxin
Ligases
Join two large biomolecules, often of the same type
Isomerases
Catalyze the interconversion of isomers, including both constitutional and stereoisomers
Lyases
Catalyze cleavage without the addition of water and without the transfer of electrons; the reverse reaction (synthesis) is usually more biologically important
Hydrolases
Catalyze cleavage with the addition of water
Oxidoreductases
Catalyze oxidation reduction reactions that involve electron transfer.
Transferases
Transfer function groups between molecules
Enzyme Mechanisms
Enzymes lower the activation energy of the reaction, thereby increasing the rate (kinetics) without altering the thermodynamics (∆G, ∆H) or the equiibrium
Competitive Inhibition
Binds to active site, raises Km, no change to Vmax
Noncompetitive Inhibition
Binds to allosteric site (present regardless of substrate); no change to Km, Vmax lowered
Mixed inhibtion
Binds to allosteric site, Km increases or decreases, Vmax lowered
Uncompetitive Inhibition
Binds to allosteric site (present only when substrate is bound); Km decreases, Vmax lowered
Michaelis-Menten Curve
Reaction velocity vs. Substrate concentration; Vmax is asymptote, Km is [S] when v = 1/2 Vmax
Lineweaver-Burk Plot
Y intercept is 1/vmax, X intercept i -1/Km; cooperative enzymes show a sigmoidal curve
3, 4, 5 carbons sugars
triose, tetrose, pentose
Aldose
Sugars with aldehydes as their most oxidized group
Ketose
Sugars with ketones as their most oxidized group
Chirality of Sugars
If the highest numbered chiral carbon with an OH group is on the right –> D; if left –> L
Enantiomers
Differ at all chiral centers
Diastereomers
Differ at at least one - but not all - chiral centers
Epimer
Differ at exactly one chiral center (type of diastereomer)
Anomer
A type of epimer that differs at the anomeric carbon
Anomeric carbon
When a sugar cyclizes, this carbon takes on either alpha or beta conformation and is a new chiral center; the carbon containing the carbonyl in the straight chain form
Alpha vs Beta sugars
alpha anomers: have the -OH on the anomeric carbon trans to the free -CH2OH group
beta anomers: have the -OH on the anomeric carbon cis to the free -CH2OH group
Mutarotation
Process by which one anomer shifts to another with the straight chain form as an intermediate
Reactions of monosaccharides
Redox; esterification; glycoside formation (basis for building complex carbohydrates and requires anomeric carbon to link to another sugar)
Deoxy sugars
Sugars with an -H replacing and -OH
Sucrose
glucose-alpha-1,2-fructose
Lactose
galactose-beta-1-4-glucose
Maltose
glucose-alpha-1,4-glucose
Cellulose
Main structural component of plant cell walls; main source of fiber in the human diet
Starches (amylose and amylopectin)
Main energy storage forms for plants
Glycogen
A major energy storage form for animals
Nucleoside
Five carbon sugar bound to a nitrogenous base
Nucleotide
A nucleoside with 1-3 phosphate groups added
Purines
Adenine and guanine; double-ringed
Pyrimadines
Cytosine, uracil, and thiamine; single-ringed
Differences between Euk/Prok replication
Euk: Nucleotides added by DNA polymerases alpha and delta, RNA primers removed by RNase H, primers replaced by DNA polymerase delta; has telomeres synth by telomerase
Prok: Nucleotides added by DNA polymerase III, RNA primers removed and replaced by DNA polymerase I
Nucleosome
When DNA is wound around histones
Heterochromatin
Dense, transcriptionally silent, DNA
Euchromatin
Less dense, transcriptionally active DNA
Genomic Library
Contains large fragments of DNA, including introns; cannot be used to make recombinant proteins or for gene therapy
cDNA library
Contains smaller fragments of DNA only including the exons of genes expressed by the sample tissue; can be used to make recombinant proteins or for gene therapy
Start codon
AUG
Stop codons
UAA, UGA, UAG
What helps prevent mutations from affecting codons?
Redundancy and wobble
Nonsense mutations
Premature stop codon
Missense mutations
Produces a codon that codes for a different AA
Frameshift mutations
Result from nucleotide addition or deletion and change the reading frame of the subsequent codons
RNA is structurally similar to DNA except:
Ribose instead of deoxyribose, uracil for thiamine, single stranded instead of double stranded
Steps in transcription
1) DNA helicase and topoisomerase unwind the double helix
2) RNA pol II binds to the TATA box in the promoter region of the gene (25 bp upstream of first transcribed base)
3) hnRNA is synthesized from antisense strand of DNA
4) 5’ cap and poly-A tail added
5) Spliceosome removes introns and ligates exons together
Transation Stages
1) initiation
2) elongation
3) termination
4) posttranslational modifications including: folding by chaperones, formation of quaternary structure, cleavage of proteins or signal sequences, and covalent addition of other biomolecules
Difference between promoters and enhancers (eukaryotes)
Promoters are within 25 bp of the first transcription site, enhancers are farther upstream than 25 bp
Osmotic Pressure
The pressure applied to a pure solvent to prevent osmosis; π = iMRT where i is the van’t hoff factor
Passive Transport
Movement of molecules down concentration gradient w/o ATP
1) simple diffusion - small nonpolar molecules do not req. transporters
2) osmosis - the movement of water across selectively permeable membrane
3) facilitated diffusion - uses transport proteins to move impermeable solutes across the cell membrane
Active Transport
Requires energy in the form of ATP (primary) or an existing favorable gradient (secondary) –> secondary can be symport or antiport
Endocytosis and Exocytosis
Both methods of engulfing material into cells or releasing material to the exterior of cells, both via the cell membrane
Pinocytosis and Phagocytosis
The ingestion of liquid and solid, respectively, into the cell from vesicles formed from the cell membrane
Glycolysis location and yield
Cytoplasm of all cells; 2 ATP per glucose