What is the net charge of Cysteine at pH 7?
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0
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What is the net charge of Cysteine at pH 7?
0
What is the structure that contains a thioether?
Thioether.
What are the abundant elements in the chemical composition of life?
Carbon, hydrogen, oxygen, and nitrogen.
What vitamin is required for the formation of hydroxyproline residues?
Vitamin C.
What is the final form of a protein after folding?
The final stable and functional tertiary structure.
What does 'R' represent in organic chemistry?
Any carbon-containing group.
What type of molecules are most amino acids?
Chiral molecules.
What are essential elements?
Elements that are necessary for the survival of living organisms.
What does Hb S stand for?
Hemoglobin S, found in sickle cells.
What type of helix does a collagen polypeptide form?
Left-handed helix.
What are amino acids composed of?
Amino group, carboxyl group, hydrogen atom, and an R group.
How does hemoglobin (Hb) behave at low pO2 (~20 - 30 torr)?
O2 is released from Hb with lower O2 affinity.
What is the function of the heme group in myoglobin?
For oxygen binding (reversible).
What bonds allow for rotation in proteins?
N - Cα and Cα - C bonds.
What type of bond connects the amino acids in the peptide 'ARVHDQ'?
Peptide bonds.
What wavelength is commonly used to estimate protein concentrations?
280 nm.
What are trace elements?
Elements required by living organisms in minute amounts.
What is the oxygen binding characteristic of myoglobin (Mb)?
Myoglobin binds oxygen with high affinity even at low pO2 in tissues.
What are β-strands?
Portions of a polypeptide chain that are fully extended.
What is the difference between the words 'kitchen' and 'thicken' in the context of amino acid sequence?
The difference lies in the sequence of letters, which can change meaning, similar to how amino acid sequence affects protein function.
How many amino acids normally occur in proteins?
20 amino acids.
What are β-sheets?
Pleated sheet structures found in proteins.
What is the structure of a collagen molecule?
Triple helix with a right-handed twist.
What defines the primary structure of a protein?
The sequence of amino acid residues linked by peptide bonds.
What is an example of a polar, uncharged R group?
Amide.
What is the maximum UV light absorption wavelength for Tyr and Trp?
280 nm.
What is the significance of the glutamate to valine mutation in hemoglobin?
It leads to the formation of sickle-shaped red blood cells.
What type of R groups are characterized as nonpolar and aliphatic?
Nonpolar, aliphatic R groups.
What is the Kjeldahl method used for?
It is used to determine the protein content in food.
What type of bonding occurs between polypeptide chains in a triple helix?
Inter-polypeptide hydrogen bonding.
How does the tensile strength of collagen compare to steel?
Collagen is stronger than steel on a per-weight basis.
What are the components of the β-sheet structure?
Cα, C, O, R, N.
What is the chemical formula for acetic acid?
CH₃COOH
Where are disulfide bridges commonly found?
In extracellular proteins.
What type of R groups are polar and uncharged?
Amide and thiol.
What is the characteristic of negatively charged R groups in terms of solubility?
They are hydrophilic.
What is the sequence of the peptide 'ARVHDQ'?
Alanine-Arginine-Valine-Histidine-Aspartic acid-Glutamine.
What type of R groups are characterized as nonpolar and aliphatic?
Nonpolar, aliphatic R groups.
What is the structure of collagen molecules?
Collagen molecules form triple helices that aggregate in a staggered manner.
What does a phylogenetic tree of cytochrome c represent?
It illustrates the evolutionary relationships among different species based on their protein sequences.
Which atoms are involved in the rotation of peptide bonds?
N, C, and Cα atoms.
What is the net charge of aspartate at pH 1?
+1
What are loops in protein structure?
Longer strands of amino acid residues linking β-strands and α-helices.
How does polypeptide diversity affect protein function?
Different polypeptide structures can lead to different biological activities and interactions.
What is a homodimer?
A protein complex formed by two identical polypeptide subunits.
What does 'L' stand for in stereochemistry?
Levo (left).
What is a heterotetramer?
A protein complex formed by four polypeptide subunits that are not all identical.
What defines a polypeptide?
A chain of more than 40 amino acids with a molecular weight of less than 10,000.
What is formed between polypeptides of adjacent triple helices?
Linkage.
What is the structure of a collagen polypeptide?
Extended and narrow chain.
What type of protein is collagen?
A structural protein in connective tissues.
What is the significance of the R group in amino acids?
The R group determines the specific properties and identity of each amino acid.
What do thousands of collagen molecules form?
Collagen fibers.
What functional group is associated with thiol R groups?
Sulfhydryl group (-SH).
How does the binding of one O2 molecule affect hemoglobin?
It facilitates the binding of the second O2 molecule.
What type of enantiomers are the chiral amino acids that occur in proteins?
L-enantiomers.
In what form are all the ionizable groups shown?
In protonated forms.
What are essential amino acids?
Amino acids that cannot be synthesized by the body and must be obtained from the diet.
What factors contribute to polypeptide diversity?
Amino acid sequence variations, post-translational modifications, and folding patterns.
How many α helices are present in each α chain of hemoglobin?
7 α helices.
What types of forces hold the subunits together in quaternary structure?
Forces similar to those in tertiary structure determination.
What role do post-translational modifications play in polypeptide diversity?
They can alter the function, activity, and stability of the polypeptide.
What is aspartame?
An artificial sweetener.
What are the two ionizable groups in free amino acids?
α-carboxyl group and α-amino group.
What is the net charge of histidine at pH 3?
+1.
What ion is associated with positively charged R groups?
Guanidinium ion.
What type of structure is the α-helix?
A right-handed helical structure.
What type of residues are modified to form cross-links?
Lysine residues.
How many polypeptides make up a collagen molecule?
Three tightly packed polypeptides.
What type of R groups are negatively charged?
Hydrophilic R groups.
What type of R groups do Tyr and Trp have?
Aromatic R groups.
What type of mutation causes Sickle Cell Anemia?
A single mutation in the β-chain.
What is the structure of a collagen molecule?
A triple helix of 3 polypeptide chains.
What is the reason some amino acids have three pKa values?
The presence of an ionizable R group.
What is the appearance of a β-sheet?
Pleated.
What is polypeptide diversity?
The variation in the sequence and structure of polypeptides, which can lead to different functions and properties.
What is the primary level of protein structure?
The sequence of amino acids in a polypeptide chain.
What is the protein conversion factor for meat?
6.25
What type of R groups are positively charged and hydrophilic?
Positively charged R groups.
What are the pKa values for histidine?
pKa1 = 1.8, pKa2 = 6.0, pKa3 = 9.3.
What happens to acetic acid when the pH is less than its pKa?
It is mostly protonated.
What is the quaternary level of protein structure?
The assembly of multiple polypeptide chains into a functional protein complex.
What is the structure that contains an imidazole ring?
Histidine.
What is the significance of the tertiary structure in proteins?
It determines the protein's function and specificity.
What does pK2 represent in the titration curve for alanine?
The pKa for the α-amino group, which is positively charged when protonated.
What is the basic building block of proteins?
Amino acids.
What type of bonding occurs within the polypeptide backbone of an α-helix?
Hydrogen bonding.
What is the protein conversion factor for soybean?
5.71
What feature of hemoglobin S contributes to its interaction?
Hydrophobic patch.
At what pH does the concentration of Form II equal the concentration of Form III?
At pH = pK2.
What is an example of a globular protein?
Triose phosphate isomerase.
What is the pK3 value for Cysteine?
10.8
What are conservatively substituted residues?
Residues that have similar R group structure and properties.
What is the role of disulfide bridges in proteins?
They help prevent protein unfolding.
What amino acid residues are formed from proline in collagen?
Hydroxyproline residues.
Which other amino acid residues are present in collagen besides proline?
Lysine and glycine.
What is the conformation of a peptide bond?
It has a partial double bond character.
How are β-sheets formed?
By hydrogen bonding between amide hydrogen and carbonyl oxygen in adjacent strands.
What are myoglobin and hemoglobin classified as?
Oxygen-binding proteins.
What is steric interference in the context of protein structure?
It refers to the spatial arrangement of atoms that can hinder rotation around bonds.
What type of residues are prominent in the sandwich structure of grass pollen protein?
Hydrophobic residues.
What is the result of the reaction between the carboxyl group and amino group of adjacent amino acids?
Formation of a peptide bond.
What type of ring structure is pyrrolidine?
A five-membered ring containing nitrogen.
Can the body produce essential amino acids?
No, they must be obtained through food.
What defines the tertiary level of protein structure?
The overall three-dimensional shape of a polypeptide, formed by interactions between R groups.
What is the primary function of myoglobin?
To store and transport oxygen in muscle tissues.
What type of protein structure does hemoglobin exhibit?
Tertiary structure.
What ions are produced when acetic acid dissociates?
H⁺ and CH₃COO⁻.
What are the components of aspartame?
Synthetic dipeptide of phenylalanine methyl ester and aspartate.
What is required for the formation of covalent cross-links in collagen?
The oxidation of lysine residues.
What do K1 and K2 represent in amino acid ionization?
Dissociation constants (Ka) for the α-carboxyl group and α-amino group, respectively.
What is the pK3 value for Arginine?
12.5
How do cross-links in collagen change with age?
They increase in number.
Can side chains involved in tertiary structure be far apart in the primary sequence?
Yes, they may be very far away in the primary sequence.
How is the protein content calculated from nitrogen content in food?
1 gram of N measured = 1/0.16 = 6.25 g of protein.
What is the relationship between pH and K_a?
At pH = pK_a, the concentration of proton acceptor equals the concentration of proton donor.
What are variable residues?
Residues that have different properties across species.
What is a characteristic feature of proteins?
Proteins have hydrophobic cores.
What are disulfide bridges?
Covalent linkages between cysteine residues within or between polypeptide chains.
What does absorbance at 280 nm indicate?
It can be used to estimate protein concentrations in solutions.
What does it mean for a molecule to be chiral?
It means the molecule has non-superimposable mirror images.
What are proteins with more than one polypeptide called?
Oligomers.
What is the initial form of a protein after synthesis?
A newly synthesized polypeptide.
What is the term for the quaternary structure of proteins?
The arrangement of multiple polypeptide chains.
What is the structural form of collagen?
A fibrous protein.
What type of protein is myoglobin?
Monomeric (1 polypeptide chain).
What is more important in determining the features of proteins: sequence or composition of amino acid residues?
Sequence of amino acid residues is more important.
What is the triplet repeat sequence commonly found in collagen?
G - X - Y (usually X=proline, Y=hydroxyproline).
What type of mutation occurs in the β-chain of hemoglobin S?
A mutation from glutamate to valine.
What is the significance of the sequence Gly-Pro-Hyp in collagen?
It is a repeating unit in collagen polypeptides.
Which letters represent the negatively charged R groups?
α, β, γ.
What do some amino acids have that is significant for their properties?
Three pKa values.
What is the conformation of the peptide group?
It forms a single plane.
What does the color blue represent in terms of hydrophobicity?
Highly hydrophobic.
Which amino acid is replaced in the β-chain mutation associated with Sickle Cell Anemia?
Glutamate is replaced by valine.
What are the two types of β-sheets?
Parallel and antiparallel.
What is one of the primary uses of melamine?
Plastic production.
What does the color green indicate regarding hydrophobicity?
Moderately hydrophobic.
What do peptide bonds link together?
Amino acids in peptides and proteins.
What is the significance of the peptide 'ARVHDQ' in protein structure?
It represents a specific sequence of amino acids that can influence protein folding and function.
What type of fibers are collagen fibers?
Insoluble fibers with tremendous tensile strength.
How can the 20 amino acids be grouped?
According to the chemical nature of their side chains (R groups).
In which secondary structure are turns commonly found?
In anti-parallel beta-sheets.
What is the structure of hemoglobin?
Heterotetramer composed of 2 α chains and 2 β chains.
What is the relationship between amino acids and the conversion factor in the Kjeldahl method?
Foods with higher percentages of specific amino acids have a smaller conversion factor.
What health risks are associated with melamine consumption?
Toxic effects, such as kidney stones.
Which amino acid residue is typically involved in inter-polypeptide hydrogen bonding in a triple helix?
Proline.
What is the quaternary structure of a protein?
The organization and arrangement of polypeptides (subunits) in a protein.
How can protein sequences be used in evolutionary studies?
By comparing sequences, scientists can infer evolutionary relationships and lineage divergence.
What is a common example of a protein with a tertiary structure?
Myoglobin.
What type of binding does hemoglobin exhibit?
Cooperative binding of oxygen into the four heme groups.
What is the shape of the oxygen binding curve for hemoglobin?
Sigmoidal curve.
What does a smaller conversion factor in the Kjeldahl method indicate?
It indicates that the food has a higher percentage of certain amino acids.
What type of protein structure is associated with grass pollen?
Sandwich structure of the β-sheets.
What is the structure that contains a thioether?
Thioether.
What is cytochrome c?
A protein involved in the electron transport chain and cellular respiration.
What is an imino acid?
An amino acid that contains a double bond between the nitrogen and carbon.
What is the net charge of aspartate at pH 5?
0
What is the protein conversion factor for milk?
6.38
Which enzyme is known for its tertiary structure?
Lysozyme.
Why are branched-chain amino acids important?
They play a crucial role in muscle metabolism and energy production.
What is a common consequence of protein misfolding?
Aggregation of proteins, leading to cellular dysfunction.
What does pK1 represent in the titration curve for alanine?
The pKa for the α-carboxyl group, which is negatively charged when deprotonated.
What strengthens collagen fibers?
Covalently cross-links.
What is the protein conversion factor for rye?
5.83
What is the protein conversion factor for whole kernel wheat?
5.83
What role do disulfide bonds play in tertiary structures?
They help stabilize the protein's three-dimensional shape.
Which carbonyl oxygen forms a hydrogen bond in the α-helix structure?
The carbonyl oxygen of residue n forms a bond with the amide hydrogen of the n+4 residue.
What is the protein conversion factor for peanuts?
5.46
What modification occurs to lysine residues to form cross-links?
They are modified to form allysine residues.
What is the pK2 value for Cysteine?
8.3
Why does proline (P) interfere with the α-helical structure?
It cannot donate an amide hydrogen bond and its side chain interferes sterically.
Which species are mentioned in relation to cytochrome c proteins?
Mammals, other vertebrates, insects, and plants.
What process transforms a newly synthesized polypeptide into a functional protein?
Protein folding.
What is the nitrogen content by mass in melamine?
67%.
Which amino acid contains an indole group?
Tryptophan (Trp).
What are turns in protein structure?
A few amino acid residues (usually 1 proline) causing an abrupt change in direction.
What type of ring structure is pyrrolidine?
A five-membered ring containing nitrogen.
How many essential amino acids are there?
Nine essential amino acids.
What stabilizes collagen fibers?
Hydrogen bonding and covalent cross-links.
What is the significance of cytochrome c in phylogenetics?
It is highly conserved across species, making it useful for studying evolutionary relationships.
What is the net charge of aspartate at pH 7?
-1
How do the tertiary structures of hemoglobin's chains compare to myoglobin?
Each α chain or β chain is very similar to myoglobin in their tertiary structures.
What is the result of the interaction between hemoglobin S molecules?
Strand formation.
What are the simplest forms of carbohydrates?
Monosaccharides.
What molecule does myoglobin bind to for oxygen transport?
Heme, which contains an iron atom that binds oxygen.
What is the charge of the α-carboxyl group at physiological pH?
Negatively charged.
What is the net charge of histidine at pH 10?
-1.
What type of chain is involved in hemoglobin S and A?
β chain.
What are the building blocks of nucleic acids?
Nucleotides.
What happens if phenylketonurics consume excess phenylalanine?
They accumulate toxic metabolites.
What can toxic metabolites from excess phenylalanine cause?
Mental retardation.
Which amino acids are classified as aliphatic?
Alanine (A), Glycine (G), Isoleucine (I), Leucine (L), and Valine (V).
What is the formula for K_a in terms of concentrations?
K_a = [H⁺][proton acceptor]/[proton donor].
What does the equation imply when pH equals pK_a?
The concentrations of proton donors and acceptors are equal.
What is the saturation level of hemoglobin with O2 in the lungs?
95% saturated with O2 at pO2 ~ 100 torr.
What significant health issue was associated with melamine in 2008?
Protein adulteration in milk products in China.
What connects the peptide groups in a β-sheet?
Peptide bonds.
What type of enzyme is horse liver alcohol dehydrogenase?
A water soluble enzyme.
What characterizes the secondary level of protein structure?
The folding or coiling of the polypeptide chain into alpha helices or beta sheets.
What is the role of proline in turns?
Proline is commonly found in turns, contributing to the abrupt change in direction.
What is the protein conversion factor for barley?
5.83
What is the net charge of histidine at pH 1?
+2.
What is the net charge of aspartate at pH 10?
-2
What does 'D' stand for in stereochemistry?
Dextro (right).
What is the tertiary structure of a protein?
The 3-D shape of a protein, including regular and irregular secondary structures.
What are complex carbohydrates made of?
Polysaccharides.
What is the isoelectric point (pI) for alanine?
6.15, the pH at which the net charge is 0.
What do covalent linkages connect in collagen?
Adjacent chains and adjacent triple helices.
What are the termini of a peptide chain?
N-terminus (amino end) and C-terminus (carboxyl end).
What is the net charge of Arginine at pH 7?
+1
What is the pK1 value for Cysteine?
1.7
What does a ribbon diagram represent?
The helices and sheets in the protein structure.
What is the final step in the Kjeldahl method?
Titration with a standard acid (e.g., HCl).
How is Sickle Cell Anemia inherited?
By inheriting the gene mutation from both parents (homozygous).
What does the color red signify?
Charged.
What is the protein conversion factor for eggs?
6.25
What is released during the formation of a peptide bond?
Water (H2O).
What is the role of glycine in the inter-polypeptide hydrogen bonding of a triple helix?
The N-H group of glycine forms hydrogen bonds with the C=O of an adjacent amino acid residue.
How many α helices are present in each β chain of hemoglobin?
8 α helices.
What are the four major types of biomolecules?
Amino acids, carbohydrates, nucleotides, and lipids.
What are the building blocks of proteins?
Amino acids.
Where is the oxygen binding site located in myoglobin?
In the heme group within the myoglobin structure.
What are the three major types of biological polymers?
Proteins (polypeptides), polysaccharides, and nucleic acids (polynucleotides).
How do BCAAs benefit athletes?
They may help reduce muscle soreness and fatigue during exercise.
Which amino acids have positively charged R groups?
Lysine, Arginine, and Histidine.
What are the basic units of lipids?
Fatty acids.
Who are phenylketonurics?
Individuals defective in phenylalanine degradation.
What is the significance of the hydrophobic patch in hemoglobin S?
It facilitates the interaction and strand formation.
What type of linkage occurs between polypeptides within the collagen triple helix?
Covalent linkage.
What are the aromatic amino acids mentioned?
Phenylalanine (F) and Tyrosine (Y).
What substitution is made to express [H⁺] in terms of pH?
Substituting pH = -log[H⁺].
What is an imino acid?
An amino acid that contains a nitrogen in a ring structure, such as pyrrolidine.
What are branched-chain amino acids (BCAA)?
A group of three essential amino acids: leucine, isoleucine, and valine.
What diseases are associated with improperly folded proteins?
Diseases such as Alzheimer's, Parkinson's, and Huntington's.
What are the two types of carbohydrates?
Monosaccharides (sugars) and polysaccharides.
What is the protein conversion factor for rice?
5.95
What is the molecular weight characteristic of proteins?
Higher molecular weights than polypeptides.
What is the pK2 value for Arginine?
9.0
How is the tertiary structure of proteins stabilized?
By non-covalent interactions between side chains of amino acid residues.
At what pH does the concentration of Form I equal the concentration of Form II?
At pH = pK1.
What is the significance of the n+4 residue in the α-helix?
It is the residue that forms a hydrogen bond with the carbonyl oxygen of residue n.
What type of amino acids are more commonly found in α-helical structures?
Small and simple amino acids.
What does K_a represent in the context of acid-base chemistry?
Dissociation constant.
What are invariant residues in cytochrome c proteins?
Residues that remain unchanged across different species (e.g., positions 9, 14, 18, 22).
What can occur when proteins fold improperly?
They can lose their functional shape and activity.
What configuration do peptide bonds typically have?
Trans configuration.
At what pH are R groups positively charged?
At pH < 6.
What are oligopeptides?
Peptides consisting of a few amino acids, such as dipeptides, tripeptides, and tetrapeptides.
What warning statement is associated with aspartame?
“Phenylketonurics: contains phenylalanine.”
How does improper protein folding affect cellular processes?
It can disrupt normal cellular functions and lead to cell death.
What is the pK1 value for Arginine?
2.2
What are the two types of hemoglobin mentioned?
Hemoglobin S and Hemoglobin A.
What is a key characteristic of BCAAs?
They have a branched molecular structure.
What do the side chains (R-groups) of amino acids project outward from?
The backbone of the amino acid.
What are disulfide bridges?
Covalent linkages formed between cysteine residues after protein folding.
Which amino acids are positively charged?
Lysine (K) and Arginine (R).
What is produced during the digestion step of the Kjeldahl method?
(NH4)2SO4.
What color represents the side chains in the α-helix structure?
Purple.
What does the amount of H+ required in titration indicate?
It is equivalent to the concentration of nitrogen in the original sample.
What role do side chains play in a β-sheet?
They extend from the peptide backbone and contribute to the sheet's stability.
Why are essential amino acids important?
They are crucial for protein synthesis and overall health.
What occurs when the pH is greater than the pKa of acetic acid?
It is mostly deprotonated.
What is the charge of the α-amino group at physiological pH?
Positively charged.
What is the net charge of histidine at pH 7?
What role do chaperone proteins play in protein folding?
They assist in the proper folding of proteins and prevent misfolding.
What does digestion of aspartame release?
Phenylalanine, methanol, and aspartate.
What is the Kjeldahl method used for?
Protein measurement in the food industry.
Which amino acids are negatively charged?
Aspartate (D) and Glutamate (E).
What is the process by which the body converts food into energy?
Metabolism.
What are the polar, uncharged amino acids?
Asparagine (N), Glutamine (Q), Serine (S), and Threonine (T).
How does glycine (G) affect the α-helical structure?
It destabilizes the structure due to unconstrained bond rotation around its α-carbon.
What is the first step in solving for [H⁺] in the K_a equation?
Solving for [H⁺] in the equation K_a = [H⁺][proton acceptor]/[proton donor].
What are stereoisomers?
Compounds that have the same molecular formula but differ in the spatial arrangement of atoms.
Are there any intra-polypeptide hydrogen bonds in a triple helix?
No, there are no intra-polypeptide hydrogen bonds.
What is the protein conversion factor for corn (maize)?
6.25
Which three amino acids are classified as BCAAs?
Leucine, isoleucine, and valine.
What occurs after strand formation in hemoglobin S?
Alignment and crystallization (fiber formation).
What are enantiomers?
A pair of stereoisomers that are mirror images of each other.
What does the tertiary structure involve?
The overall folding of the peptide backbone and the spatial arrangement of all side chains.
What is a tetrapeptide?
A peptide consisting of four amino acids, such as the sequence EGAK.
What is the significance of the oxygen binding site in myoglobin?
It enables myoglobin to effectively capture and release oxygen as needed by muscle cells.
What type of measurement does the Kjeldahl method provide?
Indirect measurement of nitrogen content.
What is the first step in the Kjeldahl method?
Digestion of organically bound nitrogen with H2SO4.
Which type of amino acids are less common in α-helical structures?
Bulky amino acids.
What is the role of boric acid (H3BO3) in the Kjeldahl method?
It reacts with NH3 to form NH4+ and the borate ion (H2BO3-).
What is the significance of pK_a in acid-base chemistry?
pK_a is the negative logarithm of the dissociation constant K_a.
Can you name a structural protein that has a tertiary structure?
Collagen.
What is the significance of the R group in amino acids?
It determines the specific properties and classification of the amino acid.
What type of biomolecule are lipids classified as?
One of the four major types of biomolecules.
What is the pKa value for the α-amino group of alanine?
9.9.
In the α-helix diagram, what color represents the carbon atoms?
Light gray for Cα and dark gray for C=O carbon.
What occurs during the neutralization step of the Kjeldahl method?
(NH4)2SO4 reacts with NaOH to produce NH3, H2O, and Na2SO4.
Are glycine (G) and proline (P) common in α-helices?
No, they are not common within an α-helix.
How does myoglobin's structure facilitate oxygen binding?
Its globular structure allows for a specific binding site for oxygen.
What are nucleotides the building blocks of?
Nucleic acids (polynucleotides).
What is the pKa value for the α-carboxyl group of alanine?
2.4.
Are the side chains of amino acids involved in hydrogen bonds within the α-helix?
No, they are not involved in H-bonds within the helix.
Why do different food items have different protein conversion factors?
Because the nitrogen content varies; for example, eggs and meat proteins contain ~16% N.
What colors represent oxygen and nitrogen in the α-helix structure?
Red for oxygen and blue for nitrogen.
What happens when you take the logarithm of both sides of the K_a equation?
It allows for the relationship between pH and pK_a to be established.
