What are the abundant elements in the chemical composition of life?
Carbon, hydrogen, oxygen, and nitrogen.
p.51
Protein Folding and Stability
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 are essential elements?
Elements that are necessary for the survival of living organisms.
p.72
Sickle Cell Anemia and Genetic Mutations
What does Hb S stand for?
Hemoglobin S, found in sickle cells.
p.7
Amino Acids and Proteins
What are amino acids composed of?
Amino group, carboxyl group, hydrogen atom, and an R group.
p.69
Hemoglobin and Myoglobin Function
How does hemoglobin (Hb) behave at low pO2 (~20 - 30 torr)?
O2 is released from Hb with lower O2 affinity.
p.66
Hemoglobin and Myoglobin Function
What is the function of the heme group in myoglobin?
For oxygen binding (reversible).
What are trace elements?
Elements required by living organisms in minute amounts.
p.69
Hemoglobin and Myoglobin Function
What is the oxygen binding characteristic of myoglobin (Mb)?
Myoglobin binds oxygen with high affinity even at low pO2 in tissues.
p.45
Protein Structure Levels
What are β-strands?
Portions of a polypeptide chain that are fully extended.
p.38
Amino Acids and Proteins
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.
p.47
Protein Structure Levels
What are β-sheets?
Pleated sheet structures found in proteins.
p.61
Protein Structure Levels
What is the structure of a collagen molecule?
Triple helix with a right-handed twist.
p.40
Amino Acids and Proteins
What defines the primary structure of a protein?
The sequence of amino acid residues linked by peptide bonds.
p.72
Sickle Cell Anemia and Genetic Mutations
What is the significance of the glutamate to valine mutation in hemoglobin?
It leads to the formation of sickle-shaped red blood cells.
p.12
Amino Acids and Proteins
What type of R groups are characterized as nonpolar and aliphatic?
Nonpolar, aliphatic R groups.
p.22
Amino Acids and Proteins
What is the Kjeldahl method used for?
It is used to determine the protein content in food.
p.63
Protein Structure Levels
What type of bonding occurs between polypeptide chains in a triple helix?
Inter-polypeptide hydrogen bonding.
p.62
Protein Structure Levels
How does the tensile strength of collagen compare to steel?
Collagen is stronger than steel on a per-weight basis.
p.56
Protein Structure Levels
Where are disulfide bridges commonly found?
In extracellular proteins.
p.35
Amino Acids and Proteins
What is the sequence of the peptide 'ARVHDQ'?
Alanine-Arginine-Valine-Histidine-Aspartic acid-Glutamine.
p.13
Amino Acids and Proteins
What type of R groups are characterized as nonpolar and aliphatic?
Nonpolar, aliphatic R groups.
p.62
Protein Structure Levels
What is the structure of collagen molecules?
Collagen molecules form triple helices that aggregate in a staggered manner.
p.73
Amino Acids and Proteins
What does a phylogenetic tree of cytochrome c represent?
It illustrates the evolutionary relationships among different species based on their protein sequences.
p.48
Protein Structure Levels
What are loops in protein structure?
Longer strands of amino acid residues linking β-strands and α-helices.
p.37
Peptide Bonds and Polypeptides
How does polypeptide diversity affect protein function?
Different polypeptide structures can lead to different biological activities and interactions.
p.58
Protein Structure Levels
What is a homodimer?
A protein complex formed by two identical polypeptide subunits.
p.58
Protein Structure Levels
What is a heterotetramer?
A protein complex formed by four polypeptide subunits that are not all identical.
p.33
Peptide Bonds and Polypeptides
What defines a polypeptide?
A chain of more than 40 amino acids with a molecular weight of less than 10,000.
p.61
Peptide Bonds and Polypeptides
What is the structure of a collagen polypeptide?
Extended and narrow chain.
p.59
Protein Structure Levels
What type of protein is collagen?
A structural protein in connective tissues.
p.7
Amino Acids and Proteins
What is the significance of the R group in amino acids?
The R group determines the specific properties and identity of each amino acid.
p.69
Hemoglobin and Myoglobin Function
How does the binding of one O2 molecule affect hemoglobin?
It facilitates the binding of the second O2 molecule.
p.11
Amino Acids and Proteins
What are essential amino acids?
Amino acids that cannot be synthesized by the body and must be obtained from the diet.
p.37
Peptide Bonds and Polypeptides
What factors contribute to polypeptide diversity?
Amino acid sequence variations, post-translational modifications, and folding patterns.
p.58
Protein Structure Levels
What types of forces hold the subunits together in quaternary structure?
Forces similar to those in tertiary structure determination.
p.37
Peptide Bonds and Polypeptides
What role do post-translational modifications play in polypeptide diversity?
They can alter the function, activity, and stability of the polypeptide.
p.24
Amino Acids and Proteins
What are the two ionizable groups in free amino acids?
α-carboxyl group and α-amino group.
p.43
Protein Structure Levels
What type of structure is the α-helix?
A right-handed helical structure.
p.61
Peptide Bonds and Polypeptides
How many polypeptides make up a collagen molecule?
Three tightly packed polypeptides.
p.70
Sickle Cell Anemia and Genetic Mutations
What type of mutation causes Sickle Cell Anemia?
A single mutation in the β-chain.
p.59
Protein Structure Levels
What is the structure of a collagen molecule?
A triple helix of 3 polypeptide chains.
p.28
Amino Acids and Proteins
What is the reason some amino acids have three pKa values?
The presence of an ionizable R group.
p.37
Peptide Bonds and Polypeptides
What is polypeptide diversity?
The variation in the sequence and structure of polypeptides, which can lead to different functions and properties.
p.39
Protein Structure Levels
What is the primary level of protein structure?
The sequence of amino acids in a polypeptide chain.
p.15
Amino Acids and Proteins
What type of R groups are positively charged and hydrophilic?
Positively charged R groups.
p.29
Amino Acids and Proteins
What are the pKa values for histidine?
pKa1 = 1.8, pKa2 = 6.0, pKa3 = 9.3.
p.39
Protein Structure Levels
What is the quaternary level of protein structure?
The assembly of multiple polypeptide chains into a functional protein complex.
p.50
Protein Structure Levels
What is the significance of the tertiary structure in proteins?
It determines the protein's function and specificity.
p.27
Amino Acids and Proteins
What does pK2 represent in the titration curve for alanine?
The pKa for the α-amino group, which is positively charged when protonated.
p.49
Protein Structure Levels
What is an example of a globular protein?
Triose phosphate isomerase.
p.74
Amino Acids and Proteins
What are conservatively substituted residues?
Residues that have similar R group structure and properties.
p.56
Protein Structure Levels
What is the role of disulfide bridges in proteins?
They help prevent protein unfolding.
p.40
Peptide Bonds and Polypeptides
What is the conformation of a peptide bond?
It has a partial double bond character.
p.45
Protein Structure Levels
How are β-sheets formed?
By hydrogen bonding between amide hydrogen and carbonyl oxygen in adjacent strands.
p.41
Protein Structure Levels
What is steric interference in the context of protein structure?
It refers to the spatial arrangement of atoms that can hinder rotation around bonds.
p.32
Peptide Bonds and Polypeptides
What is the result of the reaction between the carboxyl group and amino group of adjacent amino acids?
Formation of a peptide bond.
p.12
Amino Acids and Proteins
What type of ring structure is pyrrolidine?
A five-membered ring containing nitrogen.
p.11
Amino Acids and Proteins
Can the body produce essential amino acids?
No, they must be obtained through food.
p.39
Protein Structure Levels
What defines the tertiary level of protein structure?
The overall three-dimensional shape of a polypeptide, formed by interactions between R groups.
p.67
Hemoglobin and Myoglobin Function
What is the primary function of myoglobin?
To store and transport oxygen in muscle tissues.
p.36
Biomolecules Overview
What are the components of aspartame?
Synthetic dipeptide of phenylalanine methyl ester and aspartate.
p.64
Protein Structure Levels
What is required for the formation of covalent cross-links in collagen?
The oxidation of lysine residues.
p.24
Amino Acids and Proteins
What do K1 and K2 represent in amino acid ionization?
Dissociation constants (Ka) for the α-carboxyl group and α-amino group, respectively.
p.49
Protein Structure Levels
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.
p.21
Metabolism Fundamentals
How is the protein content calculated from nitrogen content in food?
1 gram of N measured = 1/0.16 = 6.25 g of protein.
p.25
Metabolism Fundamentals
What is the relationship between pH and K_a?
At pH = pK_a, the concentration of proton acceptor equals the concentration of proton donor.
p.74
Amino Acids and Proteins
What are variable residues?
Residues that have different properties across species.
p.53
Protein Structure Levels
What is a characteristic feature of proteins?
Proteins have hydrophobic cores.
p.56
Protein Structure Levels
What are disulfide bridges?
Covalent linkages between cysteine residues within or between polypeptide chains.
p.19
Amino Acids and Proteins
What does absorbance at 280 nm indicate?
It can be used to estimate protein concentrations in solutions.
p.8
Amino Acids and Proteins
What does it mean for a molecule to be chiral?
It means the molecule has non-superimposable mirror images.
p.51
Protein Folding and Stability
What is the initial form of a protein after synthesis?
A newly synthesized polypeptide.
p.57
Protein Structure Levels
What is the term for the quaternary structure of proteins?
The arrangement of multiple polypeptide chains.
p.66
Hemoglobin and Myoglobin Function
What type of protein is myoglobin?
Monomeric (1 polypeptide chain).
p.38
Amino Acids and Proteins
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.
p.60
Amino Acids and Proteins
What is the triplet repeat sequence commonly found in collagen?
G - X - Y (usually X=proline, Y=hydroxyproline).
p.72
Sickle Cell Anemia and Genetic Mutations
What type of mutation occurs in the β-chain of hemoglobin S?
A mutation from glutamate to valine.
p.60
Amino Acids and Proteins
What is the significance of the sequence Gly-Pro-Hyp in collagen?
It is a repeating unit in collagen polypeptides.
p.70
Sickle Cell Anemia and Genetic Mutations
Which amino acid is replaced in the β-chain mutation associated with Sickle Cell Anemia?
Glutamate is replaced by valine.
p.45
Protein Structure Levels
What are the two types of β-sheets?
Parallel and antiparallel.
p.32
Peptide Bonds and Polypeptides
What do peptide bonds link together?
Amino acids in peptides and proteins.
p.35
Protein Folding and Stability
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.
p.62
Protein Structure Levels
What type of fibers are collagen fibers?
Insoluble fibers with tremendous tensile strength.
p.10
Amino Acids and Proteins
How can the 20 amino acids be grouped?
According to the chemical nature of their side chains (R groups).
p.48
Protein Structure Levels
In which secondary structure are turns commonly found?
In anti-parallel beta-sheets.
p.68
Hemoglobin and Myoglobin Function
What is the structure of hemoglobin?
Heterotetramer composed of 2 α chains and 2 β chains.
p.22
Amino Acids and Proteins
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.
p.23
Biomolecules Overview
What health risks are associated with melamine consumption?
Toxic effects, such as kidney stones.
p.58
Protein Structure Levels
What is the quaternary structure of a protein?
The organization and arrangement of polypeptides (subunits) in a protein.
p.73
Amino Acids and Proteins
How can protein sequences be used in evolutionary studies?
By comparing sequences, scientists can infer evolutionary relationships and lineage divergence.
p.69
Hemoglobin and Myoglobin Function
What type of binding does hemoglobin exhibit?
Cooperative binding of oxygen into the four heme groups.
p.22
Amino Acids and Proteins
What does a smaller conversion factor in the Kjeldahl method indicate?
It indicates that the food has a higher percentage of certain amino acids.
p.55
Protein Structure Levels
What type of protein structure is associated with grass pollen?
Sandwich structure of the β-sheets.
p.73
Amino Acids and Proteins
What is cytochrome c?
A protein involved in the electron transport chain and cellular respiration.
p.13
Amino Acids and Proteins
What is an imino acid?
An amino acid that contains a double bond between the nitrogen and carbon.
p.14
Amino Acids and Proteins
Why are branched-chain amino acids important?
They play a crucial role in muscle metabolism and energy production.
p.52
Protein Folding and Stability
What is a common consequence of protein misfolding?
Aggregation of proteins, leading to cellular dysfunction.
p.27
Amino Acids and Proteins
What does pK1 represent in the titration curve for alanine?
The pKa for the α-carboxyl group, which is negatively charged when deprotonated.
p.50
Protein Structure Levels
What role do disulfide bonds play in tertiary structures?
They help stabilize the protein's three-dimensional shape.
p.43
Protein Structure Levels
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.
p.64
Protein Structure Levels
What modification occurs to lysine residues to form cross-links?
They are modified to form allysine residues.
p.44
Amino Acids and Proteins
Why does proline (P) interfere with the α-helical structure?
It cannot donate an amide hydrogen bond and its side chain interferes sterically.
p.74
Amino Acids and Proteins
Which species are mentioned in relation to cytochrome c proteins?
Mammals, other vertebrates, insects, and plants.
p.48
Protein Structure Levels
What are turns in protein structure?
A few amino acid residues (usually 1 proline) causing an abrupt change in direction.
p.13
Amino Acids and Proteins
What type of ring structure is pyrrolidine?
A five-membered ring containing nitrogen.
p.11
Amino Acids and Proteins
How many essential amino acids are there?
Nine essential amino acids.
p.62
Protein Structure Levels
What stabilizes collagen fibers?
Hydrogen bonding and covalent cross-links.
p.73
Amino Acids and Proteins
What is the significance of cytochrome c in phylogenetics?
It is highly conserved across species, making it useful for studying evolutionary relationships.
p.68
Protein Structure Levels
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.
p.67
Hemoglobin and Myoglobin Function
What molecule does myoglobin bind to for oxygen transport?
Heme, which contains an iron atom that binds oxygen.
p.36
Biomolecules Overview
What happens if phenylketonurics consume excess phenylalanine?
They accumulate toxic metabolites.
p.74
Amino Acids and Proteins
Which amino acids are classified as aliphatic?
Alanine (A), Glycine (G), Isoleucine (I), Leucine (L), and Valine (V).
p.25
Metabolism Fundamentals
What is the formula for K_a in terms of concentrations?
K_a = [H⁺][proton acceptor]/[proton donor].
p.25
Metabolism Fundamentals
What does the equation imply when pH equals pK_a?
The concentrations of proton donors and acceptors are equal.
p.69
Hemoglobin and Myoglobin Function
What is the saturation level of hemoglobin with O2 in the lungs?
95% saturated with O2 at pO2 ~ 100 torr.
p.23
Biomolecules Overview
What significant health issue was associated with melamine in 2008?
Protein adulteration in milk products in China.
p.39
Protein Structure Levels
What characterizes the secondary level of protein structure?
The folding or coiling of the polypeptide chain into alpha helices or beta sheets.
p.48
Protein Structure Levels
What is the role of proline in turns?
Proline is commonly found in turns, contributing to the abrupt change in direction.
p.49
Protein Structure Levels
What is the tertiary structure of a protein?
The 3-D shape of a protein, including regular and irregular secondary structures.
p.27
Amino Acids and Proteins
What is the isoelectric point (pI) for alanine?
6.15, the pH at which the net charge is 0.
p.64
Protein Structure Levels
What do covalent linkages connect in collagen?
Adjacent chains and adjacent triple helices.
p.33
Peptide Bonds and Polypeptides
What are the termini of a peptide chain?
N-terminus (amino end) and C-terminus (carboxyl end).
p.49
Protein Structure Levels
What does a ribbon diagram represent?
The helices and sheets in the protein structure.
p.20
Metabolism Fundamentals
What is the final step in the Kjeldahl method?
Titration with a standard acid (e.g., HCl).
p.70
Sickle Cell Anemia and Genetic Mutations
How is Sickle Cell Anemia inherited?
By inheriting the gene mutation from both parents (homozygous).
p.63
Protein Structure Levels
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.
What are the four major types of biomolecules?
Amino acids, carbohydrates, nucleotides, and lipids.
p.67
Hemoglobin and Myoglobin Function
Where is the oxygen binding site located in myoglobin?
In the heme group within the myoglobin structure.
p.6
Amino Acids and Proteins
What are the three major types of biological polymers?
Proteins (polypeptides), polysaccharides, and nucleic acids (polynucleotides).
p.14
Amino Acids and Proteins
How do BCAAs benefit athletes?
They may help reduce muscle soreness and fatigue during exercise.
p.15
Amino Acids and Proteins
Which amino acids have positively charged R groups?
Lysine, Arginine, and Histidine.
p.36
Biomolecules Overview
Who are phenylketonurics?
Individuals defective in phenylalanine degradation.
p.71
Hemoglobin and Myoglobin Function
What is the significance of the hydrophobic patch in hemoglobin S?
It facilitates the interaction and strand formation.
p.74
Amino Acids and Proteins
What are the aromatic amino acids mentioned?
Phenylalanine (F) and Tyrosine (Y).
p.25
Metabolism Fundamentals
What substitution is made to express [H⁺] in terms of pH?
Substituting pH = -log[H⁺].
p.12
Amino Acids and Proteins
What is an imino acid?
An amino acid that contains a nitrogen in a ring structure, such as pyrrolidine.
p.14
Amino Acids and Proteins
What are branched-chain amino acids (BCAA)?
A group of three essential amino acids: leucine, isoleucine, and valine.
p.52
Protein Folding and Stability
What diseases are associated with improperly folded proteins?
Diseases such as Alzheimer's, Parkinson's, and Huntington's.
p.6
Carbohydrates and Lipids
What are the two types of carbohydrates?
Monosaccharides (sugars) and polysaccharides.
p.33
Amino Acids and Proteins
What is the molecular weight characteristic of proteins?
Higher molecular weights than polypeptides.
p.49
Protein Structure Levels
How is the tertiary structure of proteins stabilized?
By non-covalent interactions between side chains of amino acid residues.
p.43
Protein Structure Levels
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.
p.44
Amino Acids and Proteins
What type of amino acids are more commonly found in α-helical structures?
Small and simple amino acids.
p.74
Amino Acids and Proteins
What are invariant residues in cytochrome c proteins?
Residues that remain unchanged across different species (e.g., positions 9, 14, 18, 22).
p.52
Protein Folding and Stability
What can occur when proteins fold improperly?
They can lose their functional shape and activity.
p.33
Peptide Bonds and Polypeptides
What are oligopeptides?
Peptides consisting of a few amino acids, such as dipeptides, tripeptides, and tetrapeptides.
p.36
Biomolecules Overview
What warning statement is associated with aspartame?
“Phenylketonurics: contains phenylalanine.”
p.52
Protein Folding and Stability
How does improper protein folding affect cellular processes?
It can disrupt normal cellular functions and lead to cell death.
p.71
Hemoglobin and Myoglobin Function
What are the two types of hemoglobin mentioned?
Hemoglobin S and Hemoglobin A.
p.14
Amino Acids and Proteins
What is a key characteristic of BCAAs?
They have a branched molecular structure.
p.44
Amino Acids and Proteins
What do the side chains (R-groups) of amino acids project outward from?
The backbone of the amino acid.
p.49
Protein Structure Levels
What are disulfide bridges?
Covalent linkages formed between cysteine residues after protein folding.
p.74
Amino Acids and Proteins
Which amino acids are positively charged?
Lysine (K) and Arginine (R).
p.20
Metabolism Fundamentals
What does the amount of H+ required in titration indicate?
It is equivalent to the concentration of nitrogen in the original sample.
p.46
Protein Structure Levels
What role do side chains play in a β-sheet?
They extend from the peptide backbone and contribute to the sheet's stability.
p.11
Amino Acids and Proteins
Why are essential amino acids important?
They are crucial for protein synthesis and overall health.
p.26
Amino Acids and Proteins
What occurs when the pH is greater than the pKa of acetic acid?
It is mostly deprotonated.
p.52
Protein Folding and Stability
What role do chaperone proteins play in protein folding?
They assist in the proper folding of proteins and prevent misfolding.
p.36
Biomolecules Overview
What does digestion of aspartame release?
Phenylalanine, methanol, and aspartate.
p.20
Metabolism Fundamentals
What is the Kjeldahl method used for?
Protein measurement in the food industry.
p.74
Amino Acids and Proteins
Which amino acids are negatively charged?
Aspartate (D) and Glutamate (E).
p.74
Amino Acids and Proteins
What are the polar, uncharged amino acids?
Asparagine (N), Glutamine (Q), Serine (S), and Threonine (T).
p.44
Amino Acids and Proteins
How does glycine (G) affect the α-helical structure?
It destabilizes the structure due to unconstrained bond rotation around its α-carbon.
p.25
Metabolism Fundamentals
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].
p.9
Amino Acids and Proteins
What are stereoisomers?
Compounds that have the same molecular formula but differ in the spatial arrangement of atoms.
p.63
Protein Structure Levels
Are there any intra-polypeptide hydrogen bonds in a triple helix?
No, there are no intra-polypeptide hydrogen bonds.
p.14
Amino Acids and Proteins
Which three amino acids are classified as BCAAs?
Leucine, isoleucine, and valine.
p.71
Hemoglobin and Myoglobin Function
What occurs after strand formation in hemoglobin S?
Alignment and crystallization (fiber formation).
p.9
Amino Acids and Proteins
What are enantiomers?
A pair of stereoisomers that are mirror images of each other.
p.49
Protein Structure Levels
What does the tertiary structure involve?
The overall folding of the peptide backbone and the spatial arrangement of all side chains.
p.33
Peptide Bonds and Polypeptides
What is a tetrapeptide?
A peptide consisting of four amino acids, such as the sequence EGAK.
p.67
Hemoglobin and Myoglobin Function
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.
p.20
Metabolism Fundamentals
What type of measurement does the Kjeldahl method provide?
Indirect measurement of nitrogen content.
p.20
Metabolism Fundamentals
What is the first step in the Kjeldahl method?
Digestion of organically bound nitrogen with H2SO4.
p.20
Metabolism Fundamentals
What is the role of boric acid (H3BO3) in the Kjeldahl method?
It reacts with NH3 to form NH4+ and the borate ion (H2BO3-).
p.25
Metabolism Fundamentals
What is the significance of pK_a in acid-base chemistry?
pK_a is the negative logarithm of the dissociation constant K_a.
p.9
Amino Acids and Proteins
What is the significance of the R group in amino acids?
It determines the specific properties and classification of the amino acid.
p.6
Carbohydrates and Lipids
What type of biomolecule are lipids classified as?
One of the four major types of biomolecules.
p.43
Protein Structure Levels
In the α-helix diagram, what color represents the carbon atoms?
Light gray for Cα and dark gray for C=O carbon.
p.20
Metabolism Fundamentals
What occurs during the neutralization step of the Kjeldahl method?
(NH4)2SO4 reacts with NaOH to produce NH3, H2O, and Na2SO4.
p.44
Amino Acids and Proteins
Are glycine (G) and proline (P) common in α-helices?
No, they are not common within an α-helix.
p.67
Hemoglobin and Myoglobin Function
How does myoglobin's structure facilitate oxygen binding?
Its globular structure allows for a specific binding site for oxygen.
p.6
Nucleotides and Nucleic Acids
What are nucleotides the building blocks of?
Nucleic acids (polynucleotides).
p.44
Amino Acids and Proteins
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.
p.21
Metabolism Fundamentals
Why do different food items have different protein conversion factors?
Because the nitrogen content varies; for example, eggs and meat proteins contain ~16% N.
p.43
Protein Structure Levels
What colors represent oxygen and nitrogen in the α-helix structure?
Red for oxygen and blue for nitrogen.
p.25
Metabolism Fundamentals
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.
