Notes in Biochemistry

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Status	Last Update	Fields
Published	11/14/2024	This amino acid is {{c1::Glycine}}, the three-letter code for it is {{c1::GLY}}, and the one-letter code is {{c1::G}}.
Published	11/14/2024	This amino acid is {{c1::Alanine}}, the three-letter code for it is {{c1::ALA}}, and the one-letter code is {{c1::A}}.
Published	11/14/2024	This amino acid is {{c1::Serine}}, the three-letter code for it is {{c1::SER}}, and the one-letter code is {{c1::S}}.
Published	11/14/2024	This amino acid is {{c1::Cysteine}}, the three-letter code for it is {{c1::CYS}}, and the one-letter code is {{c1::C}}.
Published	11/14/2024	This amino acid is {{c1::Threonine}}, the three-letter code for it is {{c1::THR}}, and the one-letter code is {{c1::T}}.
Published	11/14/2024	This amino acid is {{c1::Valine}}, the three-letter code for it is {{c1::VAL}}, and the one-letter code is {{c1::V}}.
Published	11/14/2024	This amino acid is {{c1::Leucine}}, the three-letter code for it is {{c1::LEU}}, and the one-letter code is {{c1::L}}.
Published	11/14/2024	This amino acid is {{c1::Isoleucine}}, the three-letter code for it is {{c1::ILE}}, and the one-letter code is {{c1::I}}.
Published	11/14/2024	This amino acid is {{c1::Proline}}, the three-letter code for it is {{c1::PRO}}, and the one-letter code is {{c1::P}}.
Published	11/14/2024	This amino acid is {{c1::Aspartate}}, the three-letter code for it is {{c1::ASP}}, and the one-letter code is {{c1::D}}.
Published	11/14/2024	This amino acid is {{c1::Asparagine}}, the three-letter code for it is {{c1::ASN}}, and the one-letter code is {{c1::N}}.
Published	11/14/2024	This amino acid is {{c1::Glutamate}}, the three-letter code for it is {{c1::GLU}}, and the one-letter code is {{c1::E}}.
Published	11/14/2024	This amino acid is {{c1::Glutamine}}, the three-letter code for it is {{c1::GLN}}, and the one-letter code is {{c1::Q}}.
Published	11/14/2024	This amino acid is {{c1::Methionine}}, the three-letter code for it is {{c1::MET}}, and the one-letter code is {{c1::M}}.
Published	11/14/2024	This amino acid is {{c1::Lysine}}, the three-letter code for it is {{c1::LYS}}, and the one-letter code is {{c1::K}}.
Published	11/14/2024	This amino acid is {{c1::Arginine}}, the three-letter code for it is {{c1::ARG}}, and the one-letter code is {{c1::R}}.
Published	11/14/2024	This amino acid is {{c1::Phenylalanine}}, the three-letter code for it is {{c1::PHE}}, and the one-letter code is {{c1::F}}.
Published	11/14/2024	This amino acid is {{c1::Tyrosine}}, the three-letter code for it is {{c1::TYR}}, and the one-letter code is {{c1::Y}}.
Published	11/14/2024	This amino acid is {{c1::Histidine}}, the three-letter code for it is {{c1::HIS}}, and the one-letter code is {{c1::H}}.
Published	11/14/2024	This amino acid is {{c1::Tryptophan}}, the three-letter code for it is {{c1::TRP}}, and the one-letter code is {{c1::W}}.
Published	11/14/2024	In living cells, the chiral amino acids in proteins are almost exclusively {{c1::ʟ::D/L}}.
Published	11/14/2024	All ʟ-amino acids have {{c1::S::R/S}}-configurations at the α-carbon except for {{c1::cysteine}}. The sulfur atom in this amino acid's side chain inc…
Published	11/14/2024	The chiral center in the side chain of ʟ-threonine has an {{c1::R::R/S}}-configuration. The chiral center in the side chain of ʟ-isoleucine has an {{c…
Published	11/14/2024	Which of these are aliphatic amino acids? {{c1::see}}
Published	11/14/2024	Which of these are aromatic amino acids? {{c1::see}}
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Glycine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Alanine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Valine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Leucine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Isoleucine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Methionine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Phenylalanine)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Tryptophan)
Published	11/14/2024	This amino acid is {{c1::Nonpolar::Polar/Nonpolar}}. (Proline)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Serine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Threonine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Cysteine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Tyrosine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Asparagine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Glutamine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Histidine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Aspartate)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Glutamate)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Lysine)
Published	11/14/2024	This amino acid is {{c1::Polar::Polar/Nonpolar}}. (Arginine)
Published	11/14/2024	In the zwitterionic form of an amino acid, the amino group is {{c1::positively::negatively/positively}} charged, and the carboxyl group is {{c1::nega…
Published	11/14/2024	The ionizable  amino acid side chains that contain nitrogen can either be {{c1::positive::negative/positive}} or neutral, and the ionizable side…
Published	11/14/2024	Decreasing the pH of a solution below the pKa of a group of interest causes {{c1::more::less/more}} than 50% of its population to be protonated. Rais…
Published	11/14/2024	The pKa of the α-Amino group is {{c1::9.6}}. The pKa of the α-Carboxyl group is {{c1::2.2}}. The mnemonic for relative pKas of ionizable ami…
Published	11/14/2024	Every amino acid has a specific pH at which the population of amino acids, on average, has a net charge of 0. This pH is called the {{c1::isoelectric…
Published	11/14/2024	Ionizable amino acid side chains can act as nucleophiles. Fully protonated forms are {{c1::weak::weak/strong}} nucleophiles. Deprotonated forms are {…
Published	11/14/2024	Amino acids serve as the building blocks for an important class of molecules called {{c1::polypeptides}}.
Published	11/14/2024	Under physiological conditions, peptide bond formation is thermodynamically {{c1::unfavorable::unfavorable/favorable}}.
Published	11/14/2024	Most peptide bonds adopt the  {{c1::trans (Z)::cis (E)/trans (Z)}} configuration with the exception of {{c1::proline::side chain}}, which can co…
Published	11/14/2024	Biological systems synthesize the {{c1::N}}-terminus of a peptide first and grow the {{c1::C}}-terminus through the addition of amino acids afterward
Published	11/14/2024	The number of amino acid residue arrangments of a tripeptide is given by the formula: {{c1::3! (3 x 2 x 1 = 6)}}. A tetrapeptide in which any of the 2…
Published	11/14/2024	The only side chains that predominantly contribute positive charge to a peptide at physiological pH are {{c1::arginine}} and {{c1::lysine}}, and the …
Published	11/14/2024	Changes to the composition of a peptide alter its isoelectric point (pI). Addition of an amino acid residue that can carry a positive charge {{c1::in…
Published	11/14/2024	The average molecular weight of the residues in a protein is approximately {{c1::110}} Daltons (Da) per residue.
Published	11/14/2024	What type of protein structure is depicted below? ({{c1::Primary::primary, secondary, tertiary, quaternary}}).
Published	11/14/2024	The two most common protein secondary structures are {{c1::α-helices}} and {{c1::β-sheets}}, with {{c1::hydrogen}} bonds between backbone groups.
Published	11/14/2024	Most of the 20 standard amino acids are commonly found within α-helices with the exception of: {{c1::Proline}} causes kinks that destabilize a-helices…
Published	11/14/2024	What amino acids commonly make up the beta turns associated with adjacent antiparallel β-pleated sheet strands? {{c1::glycine and/or proline}}
Published	11/14/2024	The stability conferred on a protein's tertiary structure is enhanced by noncovalent interactions between hydrophilic surface amino acid side chains i…
Published	11/14/2024	Some protein tertiary structures are stabilized by a type of covalent bond: {{c1::disulfide bonds}}. These bonds form with the amino acid side chain c…
Published	11/14/2024	Disulfide bonds can be broken down by {{c1::reducing::reducing/oxidizing}} agents. Disulfide bonds {{c1::do not ::do not/do}} form in cytosolic p…
Published	11/14/2024	The tertiary structure of a protein may include several distinct regions that each fold independently and often carry out different functions. These …
Published	11/14/2024	Interactions between several polypeptide units to form a single protein is referred to as {{c1::quaternary::primary/secondary/tertiary/quaternary}} st…
Published	11/14/2024	If all subunits in the protein are identical to each other, the prefix {{c1::homo}}– is added, whereas the prefix {{c1::hetero}}– is used for protein…
Published	11/14/2024	The dominant driving force of protein folding is called the {{c1::hydrophobic}} effect.
Published	11/14/2024	The classes of proteins that arise due to the hydrophobic effect include: {{c1::See}}
Published	11/14/2024	What protein structure describes this? {{c1::Globular::Fibrous/Globular/Intrinsically disordered}}
Published	11/14/2024	What protein structure describes this? {{c1::Fibrous::Fibrous/Globular/Intrinsically disordered}}
Published	11/14/2024	What protein structure describes this? {{c1::Intrinsically disordered::Fibrous/Globular/Intrinsically disordered}}
Published	11/14/2024	Proteins can be {{c1::denatured}} by several means, including sufficiently large changes in temperature, pH, salt concentration, or the presence of c…
Published	11/14/2024	The melting temperature (Tm) of a protein is the temperature at which {{c1::half of the proteins in solution are denatured and half remain folded}}.…
Published	11/14/2024	The highly ordered fibrous structures of multiple misfolded proteins commonly seen in Alzheimers and other neurodegenerative disorders is called {{c1:…
Published	11/14/2024	Certain types of misfolded proteins can act as infectious agents that can be transmitted from one organism to another. These proteins, known as {{c1:…
Published	11/14/2024	Proteins that aid in folding newly synthesized proteins and misfolded proteins are called {{c1::chaperones/heat shock proteins}}.
Published	11/14/2024	Mutations that preserve chemical properties and are therefore less likely to affect protein function are called {{c1::conservative}} mutations. Those…
Published	11/14/2024	Phosphorylation is facilitated by a class of enzymes called {{c1::kinases}} and typically occurs on the residues {{c1::serine}}, {{c1::threonine}}, or…
Published	11/14/2024	Mutation of a serine or threonine residue to glutamate or aspartate often produces the same effect as {{c1::phosphorylation::dephosphorylation/phosph…
Published	11/14/2024	The post-translational modification of glycosylation most commonly occurs in the {{c1::lumen of the endoplasmic reticulum}} and the {{c1::Golgi appara…
Published	11/14/2024	When cytosolic proteins are misfolded or no longer needed, they are commonly modified with a {{c1::polyubiquitin}} tag, which then targets them to a…
Published	11/14/2024	Other than ubiquitination, lysine residues may also be modified post-translationally by {{c1::acetylation (addition of acetyl group)}}, which is commo…
Published	11/14/2024	A nucleophilic amino acid group (lysine, cysteine, serine side chains) attacking a carbonyl linked to long, complex hydrocarbon leads to the post-tran…
Published	11/14/2024	Proteins are sometimes synthesized in an inactive form called a {{c1::proprotein}}. The post-translational modification of proteolysis can convert the…
Published	11/14/2024	Any non–amino acid group required for protein function is called a {{c1::cofactor}}.
Published	11/14/2024	Covalently bound cofactors can be thought of as post-translational modifications. These tightly bound cofactors effectively become part of the enzyme…
Published	11/14/2024	Proteins requiring prosthetic groups may be found without these groups. In this form, these proteins are called {{c1::apoproteins}}. Upon addition of…
Published	11/14/2024	The ligand for an antibody is called {{c1::an antigen}}.
Published	11/14/2024	The specific portion of the antigen to which the antibody binds is called an {{c1::epitope}}, which may include post-translational modifications such…
Published	11/14/2024	The overall strength with which a protein binds a ligand is called its {{c1::affinity}} for that ligand. It is measured by its dissociation constant,…
Published	11/14/2024	Sites on a protein that bind ligands other than the primary ligand are called {{c1::allosteric}} sites.
Published	11/14/2024	Positive cooperativity occurs when binding interactions at one site {{c1::increase::decreases/increases}} the affinity of other sites for their ligan…
Published	11/14/2024	For cooperativity, Hill coefficient n of 1 indicates {{c1::no cooperativy occurs}}. Cooperativity of 4 indicates {{c1::perfect cooperativit…
Published	11/14/2024	Which line represents positive cooperativity? {{c1::Yellow}}
Published	11/14/2024	A protein that has binding cooperativity has a {{c1::inverted sigmoid}}-shaped curve.
Published	11/14/2024	Ligands that bind receptor proteins and induce the primary biological response are called {{c1::agonists}}.
Published	11/14/2024	As a result of signal cascades, a single agonist binding its receptor can cause the phosphorylation of thousands of proteins, yielding a large cellul…
Published	11/14/2024	{{c1::Hydrophobic}} signal molecules do not require transmembrane receptors or second messengers.
Published	11/14/2024	When the intracellular concentration of a positive ion is greater than the extracellular concentration, the membrane potential is {{c1::negative::neg…
Published	11/14/2024	At a physiological temperature of 310 K, the R, T, and F, the formula for the resting membrane potential is: \[E= {{c1::{{c1::(\frac{61.5 mV}z)*l…
Published	11/14/2024	For carrier proteins, transport of one solute in one direction is called {{c1::uniport}}.
Published	11/14/2024	For carrier proteins, transport of solutes together in one direction is called {{c1::symport}}.
Published	11/14/2024	For carrier proteins, transport of one solute into the cell while another is transported out of the cell is called {{c1::antiport}}.
Published	11/14/2024	Enzymes in theory catalyze reactions in {{c1::both directions::one direction/both directions}}.
Published	11/14/2024	The reversibility of a reaction can be determined from its ∆G, the change in free energy under ambient conditions. Reversible reactions have a ∆G of …
Published	11/14/2024	What class of enzyme would lead to this reaction mechanism? {{c1::Oxidoreductase}}
Published	11/14/2024	What class of enzyme leads to this mechanism? {{c1::Transferase}}.
Published	11/14/2024	What class of enzyme leads to this mechanism? {{c1::Hydrolase}}.
Published	11/14/2024	What class of enzyme leads to this mechanism? {{c1::Lyase}}.
Published	11/14/2024	What class of enzyme leads to this mechanism? {{c1::Isomerase}}.
Published	11/14/2024	What class of enzyme leads to this mechanism? {{c1::Ligase}}.
Published	11/14/2024	Translocases couple the movement of a {{c1::solute}} across a membrane with a {{c1::catalyzed chemical reaction (eg, ATP hydrolysis, NADH oxidation)}…
Published	11/14/2024	Ligands can bind to and unbind from proteins without being chemically changed. ligands that bind to enzymes and are subsequently chemically changed a…
Published	11/14/2024	The enzyme-substrate and enzyme-product complexes have {{c1::similar or higher::lower/higher}} free energies compared to the substrate and product al…
Published	11/14/2024	What model of enzyme binding its substrate is this showing? {{c1::Lock-and-Key model}}.
Published	11/14/2024	What model of enzyme binding its substrate is this showing? {{c1::Induced fit model}}.
Published	11/14/2024	What model of enzyme binding its substrate is this showing? {{c1::conformational selection model}}.
Published	11/14/2024	An enzyme that holds two substrates at the same time is said to form a {{c1::ternary complex}}.
Published	11/14/2024	Some enzymes bind and react with one substrate in one step—forming and releasing one product and yielding a modified enzyme as a reaction intermediat…
Published	11/14/2024	If the enzyme itself serves as the Brønsted-Lowry acid (proton donor) or base (proton acceptor), this is known as {{c1::general}} acid-base catalysis…
Published	11/14/2024	An enzyme's specific activity has the units of {{c1::U/mg}} .
Published	11/14/2024	To track purity over a purification procedure, the fold-increase in purity is calculated by {{c1::dividing the specific activity of a given ste…
Published	11/14/2024	Michaelis-Menten kinetics assumes that the enzymatic reaction is {{c1::irreversible::irreversible/reversible}}.
Published	11/14/2024	The steady state approximation of the Michaelis Menten Equation supposes that concentration of the {{c1::enzyme-substrate complex [ES]}} remains cons…
Published	11/14/2024	The Michaelis-Menten equation free ligand approximation assumes that {{c1::the substrate concentration must be orders of magnitude greater than t…
Published	11/14/2024	What are the three assumptions of Michaelis-Menten kinetics? {{c1::see}}
Published	11/14/2024	What is the Michaelis-Menten equation? V0 = {{c1::see}}
Published	11/14/2024	In Michaelis-Menten kinetics, the relationship between the KM value and affinity is {{c1::inversely correlated::inversely correlated/positively correl…
Published	11/14/2024	Vmax is achieved when all enzyme molecules are {{c1::bound to substrate (ie, enzyme is saturated)}}.
Published	11/14/2024	In Michaelis-Menten kinetics, the catalytic rate constant kcat describes {{c1::how many substrate molecules an enzyme can convert to product (or "tur…
Published	11/14/2024	As kcat increases, the catalytic efficiency {{c1::increases::decreases/increases}}. As KM increases, the catalytic efficiency {{c1::decreases::decreas…
Published	11/14/2024	In a Michaelis-Menten plot, Vmax is and KM can be determined. Identify where/how. {{c1::See}}
Published	11/14/2024	The {{c1::catalytic efficiency}} is proportional to the initial slope of a Michaelis-Menten plot.
Published	11/14/2024	In comparison of Michaelis-Menten plots, a left shift ({{c1::lower::lower/higher}} KM) implies an {{c1::increased::decreased/increased}} affinity.
Published	11/14/2024	In Michaelis-Menten kinetics, assuming that the total enzyme concentration is held constant, an increase in kcat is reflected by a vertical shift {{c1…
Published	11/14/2024	In Lineweaver-Burk plots, the Vmax is determined by the {{c1::y-intercept}} and the KM is determined by the {{c1::x-intercept}} of the graph.
Published	11/14/2024	The slope of a Lineweaver-Burk plot is {{c1::inversely::inversely/positively}} proportional to catalytic efficiency.
Published	11/14/2024	Which line shows negative cooperativity, which shows positive cooperativity, and which shows no cooperativity? {{c1::see}}
Published	11/14/2024	{{c1::Competitive}} inhibitors "compete" with the substrate for the free enzyme.
Published	11/14/2024	In competitive inhibition, the effect on Vmax is {{c1::unchanged}}. The effect on KM is {{c1::an increase}}.
Published	11/14/2024	{{c1::Uncompetitive}} inhibitors only bind the enzyme-substrate complex and thereby prevent the inhibitor-bound enzyme-substrate complex from comple…
Published	11/14/2024	In uncompetitive inhibition, the effect on Vmax is {{c1::a decrease}}. The effect on KM is {{c1::a decrease}}.
Published	11/14/2024	{{c1::Mixed}} inhibitors can bind either free enzyme or the enzyme-substrate complex to prevent the reaction.
Published	11/14/2024	In mixed inhibition, the effect on Vmax is {{c1::a decrease}}. The effect on KM is {{c1::variable (increase or decrease)}}.
Published	11/14/2024	A {{c1::noncompetitive}} inhibitor binds the free enzyme and enzyme-substrate complex with equal affinities. The effect on KM is {{c1::that it is unch…
Published	11/14/2024	The forward reactions of both reversible and irreversible enzymes may slow in response to interaction with a product. For reversible enzymes, this is…
Published	11/14/2024	Allosteric effectors bind enzymes {{c1::away from::away from/at}} the active site.
Published	11/14/2024	Proteins that are synthesized in an inactive form and then converted to an active form by proteolytic cleavage are called {{c1::proproteins}}.
Published	11/14/2024	Proproteins that generate an enzyme upon cleavage are called {{c1::zymogens}}.
Published	11/14/2024	What monosaccharide is this? {{c1::D-Glucose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Fructose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Mannose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Galactose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Ribose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Ribulose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Xylulose}}
Published	11/14/2024	What monosaccharide is this? {{c1::D-Glyceraldehyde}}
Published	11/14/2024	What monosaccharide is this? {{c1::Dihydroxyacetone}}
Published	11/14/2024	The empirical formula for a monosaccharide, (CH2O)n, can give rise to many molecular formulas depending on the value of n. Give the monosaccharide cl…
Published	11/14/2024	Monosaccharides that contain an aldehyde are called {{c1::aldoses}}, and those that contain a ketone are called {{c1::ketoses}}.
Published	11/14/2024	When carbohydrates adopt a five-membered ring conformation, they are said to be in their {{c1::furanose::X-nose}} form.
Published	11/14/2024	When carbohydrates adopt a six-membered ring conformation, they are said to be in their {{c1::pyranose::X-nose}} form.
Published	11/14/2024	How many bonds to oxygen does the anomeric carbon of a monosaccharide have when it undergoes cyclization? {{c1::Two}}
Published	11/14/2024	This is a {{c1::hexose::pentose/hexose}} and a {{c1::furanose::furanose/pyranose}}.
Published	11/14/2024	For monosaccharides, when the last chiral center has an R absolute configuration, it is a {{c1::ᴅ::ʟ/ᴅ}}-sugar, and when it has an S configuration, i…
Published	11/14/2024	Which one is L- and which one is D- Fructose? {{c1::see}}
Published	11/14/2024	For turning a Fischer projection into a Haworth projection, hydroxyl groups pointing left in Fischer point {{c1::upward::downward/upward}}. Hydroxyl g…
Published	11/14/2024	Monosaccharides may also be shown in wedge-dash form, in which any hydroxyl group that is down in a Haworth projection is a {{c1::dash::wedge/dash}},…
Published	11/14/2024	Which is the α-anomer, and which is the β-anomer?  {{c1::see}}
Published	11/14/2024	Because of mutarotation, the α and β anomers of a free monosaccharide can {{c1::interconvert and exist in equilibrium}} with each other.
Published	11/14/2024	What is the difference between a bisphosphate and a diphosphate for naming in a sugar? {{c1::The prefix bis– indicates that two different positions ea…
Published	11/14/2024	The linkage between two monosaccharides is called a {{c1::glycosidic}} bond (or a {{c1::glycosidic}} linkage).
Published	11/14/2024	One monosaccharide residue has the general formula (CH2O)n. Disaccharides have the formula {{c1::Cn(H2O)n-1}}. Trisaccharides have the formula {{c1::C…
Published	11/14/2024	Characterize the glycosidic bond of this glycan. {{c1::α-1,4}}-glycosidic bond.
Published	11/14/2024	Characterize the glycosidic bond of this glycan. {{c1::β-2,6}}-glycosidic bond.
Published	11/14/2024	Is this a reducing sugar or a non-reducing sugar? {{c1::Nonreducing sugar}}.
Published	11/14/2024	For the blue arrows, which end is the reducing end and which end is the nonreducing end? {{c1::See}}
Published	11/14/2024	What is the name of this disaccharide? {{c1::Maltose}}
Published	11/14/2024	What is the name of this disaccharide? {{c1::Sucrose}}
Published	11/14/2024	What is the name of this disaccharide? {{c1::Lactose}}
Published	11/14/2024	Polysaccharides consisting entirely of glucose units are called {{c1::starches}}. The simplest of which is shown below, called {{c1::amylose}}
Published	11/14/2024	What is the name of the starch below (branch point every ~25 glucose units)? {{c1::Amylopectin}}. If there are more branch points, it would be {{c1::g…
Published	11/14/2024	What is the name of this polysaccharide? {{c1::Cellulose}}.
Published	11/14/2024	What structure is this? {{c1::Pyrimidine}}
Published	11/14/2024	What structure is this? {{c1::Purine}}
Published	11/14/2024	What structure is this? {{c1::Guanine}}
Published	11/14/2024	What structure is this? {{c1::Cytosine}}
Published	11/14/2024	What structure is this? {{c1::Adenine}}
Published	11/14/2024	What structure is this? {{c1::Thymine}}
Published	11/14/2024	What structure is this? {{c1::Uracil}}
Published	11/14/2024	Tautomerization would lead to this molecule to look like what? {{c1::see}}
Published	11/14/2024	Tautomerization would lead to this molecule to look like what? {{c1::see}}
Published	11/14/2024	In deamination, the primary amino groups in A, G, and C are replaced by {{c1::carbonyls}}.
Published	11/14/2024	Which position is cytosine commonly methylated at? {{c1::Position 5}}
Published	11/14/2024	These structures are {{c1::ribose}} and {{c1::deoxyribose}}. They belong to a class of compounds called {{c1::nucleosides}}.
Published	11/14/2024	What structure is this? {{c1::Guanosine}}
Published	11/14/2024	What structure is this? {{c1::Deoxythymidine}}
Status	Last Update	Fields