Bio/Biochem Flashcards
im·mu·no·as·say
a procedure for detecting or measuring specific proteins or other substances through their properties as antigens or antibodies
immunoassay
An immunoassay is a biochemical test that measures the presence or concentration of a macromolecule or a small molecule in a solution through the use of an antibody (usually) or an antigen (sometimes)
what is ELISA?
enzyme-linked immunosorbent assay, an immunological assay technique making use of an enzyme bonded to a particular antibody or antigen
Direct ELISA Assay
The surface of the plate is coated directly with the sample. An enzyme-tagged antibody enables its measurement
Indirect ELISA Assay
Indirect ELISA is a two-step binding process involving the use of a primary antibody and a labeled secondary antibody
Competitive ELISA
In competitive enzyme immunoassays, the antigen in a sample competes for limited antibody binding sites with antigen conjugated to a reporter enzyme. This produces an inverse relationship between antigen concentration and substrate turnover. Competitive ELISAs typically use a single antibody to a low molecular weight antigen
capture assay
an enzyme immunoassay using two antibodies; the first binds the antigen to solid phase, and the second contains the enzyme label and acts as an indicator
A low NAD+/NADH ratio drives what?
having more reduced NADH (NAD+) drives fatty acid synthesis because NAD+ is used to generate ATP which is required for fatty acid synthesis
Tollen’s reagent
Tollen’s reagent is an oxidizing agent used to determine the presence of aldehydes and ketones *add functional groups to quizlet
DNA stop codons
TAA, TAG, TGA
RNA stop codons
UAA, UAG, UGA
add amino acids
amino acids
this amino acid can be used for gluconeogenesis
proline
Where does the Krebs cycle (also TCA cycle and citric acid cycle) occur?
mitochondrial matrix (inside)
Krebs Cycle (Citric Acid Cycle)
The Krebs Cycle, also known as the citric acid cycle, takes place in the matrix of the mitochondria. In the Krebs Cycle, each of the two acetyl coenzyme A molecules enter the cycle and combine with oxaloacetate to form citric acid, which then loses two carbons as carbon dioxide. The cycle is now ready to begin again with the second Acetyl CoA. For each Acetyl CoA, the Krebs Cycle produces 1 ATP, 3 NADH, and 1 FADH2.
Krebs cycle
breaks down glucose following glycolysis (which occurs in the cytoplasm)
Pyruvate
Three-carbon compound that forms as an end product of glycolysis. 2 pyruvate for each glucose
pyruvate has to be actively transported
from cytoplasm to matrix for krebs cycle
pyruvate dehydrogenase
converts pyruvate to acetyl-CoA (which then enters the krebbs cycle) - stimulated by insulin - inhibited by acetyl-CoA
Acetyl CoA
is a precursor for fatty acid synthesis and is generated in the mitochondria but enzymes for FA synthesis are in the cytoplasm so acetyl coA has to be changed into citrate to be transported beck into cytoplsm transforming citrate back to acetyl coA generates acetyl coA and oaxaloacetate (which can be changed into pyruvate which can be used for glycolysis)
NADPH
reducing agent to help with anabolic reactions
anabolic
building up (uses ATP)
cofactor
A nonprotein molecule or ion that is required for the proper functioning of an enzyme. Cofactors, mostly metal ions or coenzymes, are inorganic and organic chemicals that assist enzymes during the catalysis of reactions
ATP hydrolysis
energy released, loses phosphate
fatty acid oxidation
Fatty acid oxidation is the mitochondrial aerobic process of breaking down a fatty acid into acetyl-CoA units
add all orgo functional groups
orgo functional groups
Isomer
Compounds with the same formula but different structures.
amino acid residue
an amino acid in a polypeptide that is not the N or C terminal AA. This refers to every amino acid in a polypeptide chain.
fructose has a
ketone (is a ketose)
glucose, galactose, and ribose are all
aldoses
aldehydes are more reactive to oxidation than
ketones
Pyrimidines
Cytosine and Thymine
visualization of an antigen of interest in an immunoassay requires labeling of antibodies with…
- flourophores 2.enzymes 3. radioisotopes 4.biotin 5.small peptides NOT large proteins like Albumin
transmembrane proteins
two hydrophilic portions and one hydrophobic portion, provide about 50% of the drug targets
monotopic proteins
only on one side of the membrane
globular proteins
these are compact, generally rounded, and soluble in water.
fibrous proteins
long, insoluble, structural proteins.
The reduced form
a gain of H bonds and a decrease in oxidation state
tertiary structure of protein
Defined by the hydrophilic, ionic and hydrophobic interactions between R groups of amino acid chains.
secondary structure of protein
alpha helix and beta pleated sheet, determined by H bonds
primary structure of protein
the amino acid sequence of the polypeptide chain
phosphate groups
negatively-charged groups that store the energy in ATP -found in ATP, ADP, and DNA/RNA backbone
Testosterone
steroid hormone, not charged, can pass through the plasma membrane
amine hormone
Amino acids with modified groups Ex. Norepinephrine
peptide/protein hormones
-Chains of amino acids -short-acting -promote second-messenger cascades -soluble in water (polar) ex. oxytocin
protein hormone
long chains of linked amino acids ex. human growth hormone
steroid hormones
-derived from cholesterol, nonpolar -share cholesterol’s fused-ring hydrocarbon structure -signaling molecules that bind to their receptors in the nucleus and impact transcription ex. testosterone, progesterone, estrogen
Histone
protein molecule around which DNA is tightly coiled in chromatin histones are usually positively charged which attracts them to to the negative DNA backbone
ATP hydrolysis
releases energy because the ATP structure is unstable because of the close phosphate groups
insulin
A peptide/protein hormone (made of amino acids aka polar) produced and secreted by the Beta cells of the pancreas. Insulin targets cells in the body, especially the liver and muscle, and allows them to take glucose out of the blood (thus lowering blood glucose levels).
memmorize all the
amino acids
pyrimidines
can be metabolized into malonyl-coA by being fed into the citric acid cycle and used to generate NADH/FADH2
ketogenic amino acids
leucine and lysine -meaning they do not produce intermediates that can be converted to glucose
glucogenic amino acids
amino acids that can be used to form glucose They are: A, R, N, D, C, E, G, H, V, M, P, and S DARN CHEG VMPS
formation of a disulfide bond occurs through
oxidation
a carbonyl carbon is a classic ______________ due to the electron withdrawing effect of the double-bonded carbonyl oxygen
electrophile
______ is the nucleophile that attacks during the peptide bond formation
the amino terminal nitrogen
things used to denature proteins:
- heat 2.pH 3.inorganic salt solution (an enzymatic inhibitor would not be used to denature a protein)
look up gabriel synthesis
involves sn2 mechanism (look up diff between sn1 and sn2)
SN1 and SN2 https://www.masterorganicchemistry.com/2012/08/08/comparing-the-sn1-and-sn2-reactions/
SN1 involves carbocation formation which is the rate-limiting step, nucleophile can attack on either plane of sp2 C, so both enantiomers can form SN2 involves backside attack, so inversion of configuration with pentavalent transition state unimolecular nucleophilic substitution (SN1), whereby the rate determining step is unimolecular and bimolecular nucleophilic substitution (SN2), whereby the rate determining step is bimolecular SN1 on 2/3 degree carbons only (carbocation stability!), SN2 on 0/1/2 degree carbons only SN1 considerations: 1. doesn’t consider nucleophile size/conc. in rate law 2. polar, protic solvent 3. 2/3 degree carbons only SN2 like polar, aprotic solvents: acetone, DMF, DMSO alcohols and ethers undergo substitution only with an acid catalyst or conversion to a better leaving group (something resonance stabilized maybe) “Protic” Solvents Have O-H or N-H Bonds And Can Hydrogen-Bond With Themselves. “Aprotic” Solvents Cannot Be Hydrogen Bond Donors
catalytic site
reduces chemical activation energy
orthosteric regulation
regulator binds in active site
allosteric regulation
regulator binds at non-active site
oxidoreductases
catalyze oxidation-reduction reactions ex. alcohol dehydrogenase superoxide dismutase
transferases
transfer functional groups between molecules ex. aspartate transaminase creatine kinase DNA polymerase
hydrolases
catalyze hydrolysis ex. angiotensin-converting enzyme pancreatic lipase lactase
lyases
cleave bonds through non-hydrolysis mechanisms ex. pyruvate decarboxylase aconitase
isomerases
catalyze isomerization ex. ribose-5-phosphate isomerase
ligases
join molecules together with covalent bonds ex. aminoacyl tRNA synthetase glutamine synthetase pyruvate carboxylase
phosphatases _______ phosphate groups, while kinases_______ phopshate groups
remove, add
cooperativity
It amplifies the response of enzymes to substrates, sigmoidal curve
Hill coefficient
A measure of cooperative interaction between protein subunits if >1 then binding of each ligand is easier and positive cooperativity if <1 then binding of each successive ligand is harder and negative cooperativity (inhibition)
Km constant in the Michaelis-Menten equation
the concentration of substrate that corresponds to half of vmax (max velocity of the reaction)
michaelis-menton equation
V=Vmax[S]/Km+[S]
Km is important because
it can be used as a measure of the affinity that an enzyme has for its substrate
km is not affected by _______ but is affected by __________
not: the concentration of the substrate or enzyme Is: inhibitors
competitive inhibitors
-compete with the substrate -do NOT affect Vmax because by adding more substrate you can minimize the effect of the competitive inhibitor -DO affect Km because their effects can be neutralized with extra substrate, but adding the extra substrate requires more substrate to reach half of Vmax, which by definition means increasing Km
noncompetitive inhibitors
-interact with the enzyme allosterically -essentially prevent the enzyme from working -effect is similar to reducing the concentration of the enzyme that is present -DOES reduce Vmax -does NOT affect Km because the molecules of enzyme that are not affected by the noncompetitive inhibitor remain functional
uncompetitive inhibitors
-interact with the enzyme-substrate complex at an allosteric site, essentially prevent an enzyme from letting go of a substrate that it has bound -Vmax decreases bc the overall rate of the catalyzed reaction is reduced -decrease in Km because the stabilization of the E-S complex effectively means that the enzyme seems to have a greater affinity for the substrate
mixed inhibition
-inhibitor can either -can bind the free enzyme at an allosteric site or can bind the E-S complex -Vmax is always decreased -its effect on Km depends on the binding preference of a given inhibitor if prefers binding to E-S complex: similar to an noncompetitive inhibitor so Km will be decreased if prefers binding to the free enzyme at an active site (allosteric I think)**??? then Km is increased tim said: The correct answer is that a mixed inhibitor may bind the active site of the free enzyme (like a competitive inhibitor) or to an allosteric site on the enzyme-substrate complex (like an uncompetitive inhibitor (note: not the same as a non-competitive inhibitor). Depending upon the inhibitor’s “preference” for binding free E or E-S complex, you will get an effect that “mimics” a competitive or non-competitive inhibitor.
phosphorylation most commonly targets
serine, threonine, and tyrosine which all have -OH groups that the phosphate group can be attached to
zymogens or proenzymes
are produced in their inactive form and can be activated by cleavage at a later time when they are needed
cofactors or coenzymes (organic cofactors)
are required for the enzyme to be activated
Kinetic efficiency
a measure of how efficiently an enzyme converts substrates into product Kcat/Km highest ratio=highest efficiency
homogenate
a mixture of all of the components of the cell, but no intact cells.
Warberg effect
cancer cells rely on anaerobic glycolysis instead of ox phos (more efficient) to generate energy
primary active transport
Active transport that relies directly on the hydrolysis of ATP.
secondary active transport
Form of active transport which does not use ATP as an energy source; rather, transport is coupled to ion diffusion down a concentration gradient established by primary active transport.
Microfilaments
Long, thin fibers that function in the movement and support of the cell
Microtubules
Spiral strands of protein molecules that form a tubelike structure
intermediate filaments
A component of the cytoskeleton that includes filaments intermediate in size between microtubules and microfilaments.
antibody IgA
-present in mucosal areas such as the gut, respiratory tract, saliva, tears, breast milk, and the urogenital tract, -it helps prevent colonization by pathogens
antibody IgD
-principally acts as an antigen receptor on B cells that have not been exposed to antigens -it is involved in the activation of mast cells and basophils
antibody IgE
-involved in allergies and anti-parasitic responses -IgE binds to allergens, causing histamine release from activated mast cells and basophils
antibody IgG
-four forms of IgG provide most of the humoral immune response -it is the only antibody type capable of crossing the placenta and conferring passive immunity to a developing fetus
antibody IgM
-the first antibody secreted upon exposure to an antigen -responsible for mounting an immune response and eliminating pathogens in the early stages of the humoral response, before IgG levels increase -it is expressed on the surface of B cells as a monomer and is secreted by plasma cells as a pentamer
CAMs
cell adhesion molecules
Cytokines
-Chemicals released by the immune system communicate with the brain. -signaling molecules of the immune system
motor protein: Kinesins
move towards the (+) end of microtubules (towards the periphery), transport vessicles and organelles by travelling along microtubules, which requires the hydrolysis of ATP
motor protein: dyneins
carry cargo xtowards the (-) end of microtubules (towards center)
motor protein: myosin
involved in muscle contractions, use ATP to carry out power stroke
antibodies
-glycoproteins that recognize antigens (characteristic regions, usually of foreign objects/substances) -composed of at least one immunoglobulin (Ig) unit, each of which has two heavy chains and two light chains, forming a Y shape -several types exist; most important are IgM antibodies, which respond to acute infections, and IgG antibodies, which help confer lasting immunity
cell adhesion
proteins involved include selectins, cadherins, and integrins
cell adhesion: anchoring junctions
involve cadherins, help keep cells/tissues in place
cell adhesion: gap junctions
formed by connexin proteins, connect cells in a way such that diffusion/communication can take place between them
cell adhesion: tight junctions
involve several types of proeteins, are found in epithelial cells, and prevent solutes from being able to move freely from one tissue into another classic example: blood-brain barrier
ion channel-linked receptors:
-also known as ligand-gated ion channels -change shape in response to binding with a ligand to open and let ions through
enzyme-linked receptors
-either enzymes themselves, or are directly associated with the enzymes that they activate -majority are protein kinases, and regulate many normal cellular processes
G protein-coupled receptors
-composed of three distinct alpha, beta, and gamma subunits -they become activated by binding with GTP -the alpha subunit together with the bound GTP dissociates from the beta and gamma subunits, which interact with other signaling processes in the cell (secondary pathways)
nuclear receptors
-found within the cell (either on the nucleus or in the cytosol before travelling to the nucleus) and regulate gene transcription in response to binding with a signaling molecule (often a steroid hormone)
specificity constant of the interaction between two molecules
kcat/km
Kcat
turnover number (molecules catalyzed per second in optimal conditions) Vmax / [E]
actin filaments
can be assembled in a branched pattern (while microtubules cannot)
Goldberg-Hogness box (TATA box)
A short nucleotide sequence 20-30 bp upstream from the initiation site of eukaryotic genes to which RNA polymerase II binds. The consensus sequence is TATAAAA. Also known as a TATA box. promoter for transcription
kinetochore
-protein complex assembled at each centromere -serves as an attachment site for spindle microtubules and the site at which motors generate forces to power chromosome movement
spindle poles
ends of spindles (specialized microtubules that captures and separates chromosomes)
centriole
Made of bundles of long filaments called microtubules that help in organizing cell division, radiate in star-shaped clusters known as asters which help align chromosomes during cell division
Centromere
Area where the chromatids of a chromosome are attached
Immunoglobulin M (IgM) contains
two heavy chains and two light chains
cadherins
cell adhesion molecules that comprise adherens junctions and serve to connect cells to eachother (transmembrane proteins)
dyneins
require ATP, involved in retrograde transport of cargo (movement towards center of the cell)
G proteins
activated by substitution of GDP for GTP, but deactivated when GTP is hydrolyzed to GDP by GTPase
look up a video on titration
each half equivalence point signifies a functional group
look up cation exchange chromatography
In cation-exchange chromatography, positively charged molecules are selectively purified via binding to an anionic solid phase. Thus, for this amino acid to be purified in this manner, it must have a net positive charge. adding more base means the unknown amino acids will be less positive, just as a concept
linking of amino acids
Polypeptides are formed via dehydration synthesis reactions that link amino acids with peptide bonds. The incoming amino group acts as a nucleophile and attacks the carbonyl carbon, and the labeled hydrogen molecule (along with the O to which it is directly bound) is released as water.
ion exchange chromatography
Ion-exchange chromatography separates compounds based on net charge. In this case, the stationary phase is negative, meaning that positive compounds will be retained in the column. In other words, these species will elute more slowly because they will interact more with the stationary phase. Therefore, we would expect the polypeptide that elutes first to contain fewer positively-charged residues than the one that elutes second. Arginine (R) is positively charged at physiological pH, so it is unlikely to be common in the polypeptide referenced.
protein tertiary structure
Tertiary structure is driven by the tendency of hydrophobic residues to bury themselves inside the protein, away from aqueous environments, as well as side chain interactions such as hydrogen bonding and disulfide bridges. We can therefore expect that a substitution between amino acids that vary in polarity, charge, or sulfur content might change this level of structure. Of all the replacements listed, exchanging glycine (a nonpolar, neutral residue that lacks sulfur) with cysteine (a polar AA with the ability to participate in disulfide bridges) is most likely to cause a change in tertiary structure.
the only amino acid that can for disulfide bonds is… because it has…
cystein, a free -SH group
look up what makes something aromatic
Aromatic compounds are those that contain planar, conjugated rings and follow Hückel’s rule, which stipulates that the system must possess 4n + 2 π electrons. (To simplify this rule, remember that “n” denotes any integer, meaning that aromatic systems may contain 6, 10, or 14 π electrons, and so on.) Tyrosine, a classic example of an aromatic amino acid, fits all of these qualifications.
enzymes affect the ______ not the _______ of a reaction
kinetics, thermodynamics
spontaneous v non spontaneous reactions
As a rule of thumb, remember that exergonic reactions (ΔG < 0) are spontaneous, while endergonic processes (ΔG > 0) are nonspontaneous
energy-rich compunds
ATP, creatine phosphate, and acetyl-CoA are all similar in that they contain high-energy phosphate or thioester bonds. used to couple to and drive nonspontaneous reactions
second law of thermodynamics
he second law of thermodynamics states that a spontaneous reaction or cyclic process must yield a net entropy increase.
first law of thermodynamics
Energy can be transferred and transformed, but it cannot be created or destroyed.
Third Law of Thermodynamics
The entropy of a perfect crystal is zero when the temperature of the crystal is equal to absolute zero (0 K).
Gibbs free energy
ΔG = ΔH - TΔS, where ΔH represents the change in enthalpy, T denotes Kelvin temperature, and ΔS denotes the change in entropy.
ATP equivalents of NADH and FADH2
NADH=2.5ATP FADH2=1.5ATP (because FADH2 enters the ETC one complex later than NADH)
Enantiomers
isomers that are mirror images of each other, but not superimposable
which enantiomer is present in the human body
L
Anion exchange chromatography
Negative proteins stick to positive beads, only positive proteins go through (name describes what it captures/what elutes last)
pI
net charge of a protein will be zero
SDS-PAGE
Type of chromatography used to separate proteins based on mass.
Beer-Lambert Law relationship between absorbance, extinction coefficient, concentration, and path length
absorbance = εCL. Here, ε represents the extinction coefficient, C denotes the concentration of the solution, and L stands for the path length in centimeters
SDS-PAGE
breaks up proteins into its subunits
critical pont
the the concentration where the length of the polymer is sable (no net polymerization or depolarization occurs)
the ___ ends of actin molecules display stronger intermolecular interactions than the ______ ends
ERROR!
microtubules originate from
microtubule-organizing centers, or MTOCs, these structures anchor the minus end of the microtubule to prevent depolymerization, they aslo form the origin of the spindle aparatus during cell division
variable region of antibody
-antigen binding site, is specific to the antigen -includes the ends of the light and heavy chains
constant region of an antibody
the constant region determines the mechanism used to destroy antigen, this region can be recognized by other immune components to further stimulate the response to a pathogen
dynein transport
-travel toward the center of the cell -move toward the minus ends of the associated microtubules -are involved in retrograde transport
vitamin E
antioxidant. Essential for protection of cell structure, especially of red blood cells
vitamin A
regulator of tissue growth
Vitamin B
The B vitamins are the largest group of vitamins and function in the production of multiple cofactors. Biotin is a B vitamin that acts as an important coenzyme, while riboflavin serves as a structural part of the cofactors FMN and FAD
Vitamin D
influence over bone growth and calcium regulation
NAD is a
Coenzyme Coenzymes are a subset of cofactors that tend to bind loosely to their associated enzymes. This type of molecule is also known for transferring functional groups between species. NAD serves this function by donating its hydrogen to Complex I, which is one of the four protein complexes responsible for generating the proton gradient during aerobic cellular respiration.
prosthetic groups
small molecules permanently attached to the enzyme, tightly bound
Km
is simply the substrate concentration at which reaction rate is equal to one-half of the Vmax
disulfide linkages are cleaved exclusively via
oxidation/reduction reactions
SDS (of SDS-PAGE)
disrupts secondary and tertiary protein structure and applies a uniform negative charge across the protein
immunoaffinity
uses antibody-protein affinity to retain the desired substrate on the solid phase matrix
salting in
-refers to the addition of salt to a solution that does not yet contain very high salt concentrations -the salt interacts with charged amino acid side chains, reducing the protein’s ability to aggregate with other proteins -the net result is increased protein solubility
the presence of _______ amino acids in a protein cause the protein to absorb ultraviolet light whose wavelength range is: the aromatic amino acids are:
aromatic, 200-400nm Tyr, Trp, Phe
in cation exchange chromatography, ______ will elute first
anions -the stationary phase is designed to attract cations (so it is comprised of anions)
transition state
it is always is a higher energy state than the reactants or products. Thus any time the transition state is stabilized, activation energy (which by definition is the energy required to reach the transition state) is reduced. The more stable a transition state is, the less energy is required to reach it which makes it easier to go from the reactants to the final product.
Angiotensinogen
- zymogen precursor to angiotensisn, a peptide hormone that leads to vasoconstriction -produced in the liver
make flashcards for these:
FLAG TOP, PAVO, PIGS, ACAC, and THC. FLAG TOP for things coming from anterior pituitary (Fsh, Lh, Acth, Growth Hormone, Tsh, MelOncyte stimulating hormone, prolactin) for posterior pituitary I remember PAVO (Posterior, Adh/Vasopressin, Oxytocin) for the pancreas I remember PIGS (Pancreas, Insulin, Glycogen, Somatostatin) for the thyroid I remember THC like in marijuana (Thyroid Hormone, Calcitonin) and for adrenal cortex I remember ACAC (Adrenal Cortex, Aldosterone, Cortisol)
make flashcards for these hormones
These are all the hormones that must be memorized for the MCAT. Learn the 5 steroid and know the rest are protein, know where there are secreted from (in the case of oxytocin and vasopressin (or antidiuretic hormone) know they are made in the hypothalamus and secreted to the posterior pituitary where they are stored and later secreted.Steroid:Testosterone (Androgen): TestesProgesterone: Ovary specifically corpus luteumEstrogen: ovary specifically follicleAldosterone: adrenal cortexCortisol: adrenal cortexProtein:Follicle stimulating hormone: anterior pituitaryLeutinizing hormoneACTHThyroid stimulating hormone (TSH)ProlactinGrowth hormoneOxytocin: posterior pituitaryVasopressinInsulin: pancreasGlucagonParathyroid hormone: parathyroidCalcitonin: thyroidThyroxineEpinephrine: Adrenal MedullaNorepinephrine
hypophyseal portal system
blood leaving capillary beds in hypothalamus travels to a capillary bed in anterior pituitary to allow for paracrine secretion of releasing hormones
-dioic acid
2 carboxylic acids
epimers
are carbohydrates which differ in their configuration of a single chirla center
memorize carbohydrates on pg16 of bio
there is a chart
Tollen’s reagent, like Benedict’s reagent, is used to
test for reducing sugars (it oxidizes an aldehyde into a carboxylic acid) Reducing sugars have free aldehyde groups that can be oxidized to caroxylic acids, which reduces the tollens reagent to elemental silver
Anomers
specific category of epimers, which are stereoisomers that differ in only one chiral center (ex. in solution glucose readily undergoes mutarotation between its alpha and beta anomers)
specific rotation
-an experimental value -generally, the specific rotation of a particular compound does not relate in any predictable way to that of another compound except enantiomers have equal but opposite specific rotation values and racemic solutions have a specific rotation of 0 degrees
Fisher Projection
horizontal=out of the paper vertical= into the paper
enzymes have chiral active sites so
if D-glucose is normally acted on by an enzyme, that enzyme could not work on L-glucose
hemiacetal
A functional group that contains a carbon atom bonded to one -OR group, one -OH group, an alkyl chain, and a hydrogen atom.
pyranose v furanose
six-membered rings=pyranoses five-membered rings=furanoses
anomer
A sugar diastereomer differing only in the position of the hydroxyl at the anomeric carbon (the one attached to the OH)
glycosidic bond
A glycosidic bond is a covalent bond in which a carbohydrate binds to another group, which could also be a carbohydrate. A glycosidic bond is found between the two glucose molecules in maltose.
peptidoglycan
A protein-carbohydrate compound that makes the cell walls of bacteria rigid, consists of carbohydrates that have been modified with amino acids
Chitin
Polysaccharide found in arthropod exoskeletons and fungal cell walls.
optical rotation of light
d/l or +/-
absolute configuration
-R/S -determined by the 3D arrangement of the groups attached to the chiral carbon
comparing longer-chain carbohydrates to the three-carbon substance glyceraldehyde
D/L (different than the d/l system and does not have anything to do with how light is rotated)
D/L
-any carbohydrate in which the bottom most -OH in the Fisher projection is pointing right is D and pointing left is L -most carbohydrates in living organisms are D isomers
the alpha helical structure of a protein is held together by which of the following?
hydrogen bonding between carbonyl oxygen and amino hydrogen atoms
Squalene
-is a terpene, or a compound composed of isoprene (C5H8) units -do not contain oxtgens -precursor to cholesterol
family of receptors that allow glucose into the cells
GLUT receptors
GLUT 1
receptor that allows glucose into the cell -is expressed throughout the body and is responsible for constant low-level baseline glucose intake
GLUT 2
receptor that allows glucose into the cell -expressed by liver, pancreatic beta, and kidney cells -bidirectional transporter (both in and out of the cell)
Bacterial cells ______ carry out post-transcriptional modification of mRNA.
cannot
cDNA
Complementary DNA. DNA produced synthetically by reverse trascribing mRNA. Because of eukaryotic mRNA splicing, cDNA contains no inrons.
dsDNA
double stranded DNA
ssDNA
single stranded DNA
all of these are true about the major groove
I. The major groove offers more space for the enzymes to access the sides of the bases. II. In the minor groove, the enzymes would be unable to tell the difference between an A-T and a T-A pair. III. The enzymes cannot bind to phosphate groups in the DNA backbone in a sequence-specific way
What is the principle contributor to DNA helix stability?
hydrophobic effect
Western Blotting
Western blotting is a technique in which proteins are run on a gel using electrophoresis, transferred to a nitrocellulose or similar membrane, and finally washed with an antibody marker. It is typically used to determine the identity of particular proteins present in a sample and can sort these proteins by molecular weight.
Northern blots
detect the presence of mRNA, not protein.
Southern blots
identify particular DNA sequences. The question asked about the detection of protein.