Biochemistry Fundamentals

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Questions and Answers

A segment of DNA contains 30 base pairs, including 10 guanine residues. How many cytosine residues are present?

  • 30
  • 10 (correct)
  • 20
  • 40

Besides tyrosine, which amino acid shares a similar ring structure that could potentially undergo modifications to form neurotransmitters?

  • Alanine
  • Tryptophan (correct)
  • Glycine
  • Serine

Which component is absent in deoxythymidine monophosphate compared to guanosine monophosphate?

  • Phosphate group
  • Nitrogenous base
  • Ribose sugar (correct)
  • Deoxyribose sugar

A pentapeptide (5 AA) is hydrolyzed into two fragments: one dipeptide and one tripeptide. If the pentapeptide initially contained eight oxygen atoms, how many oxygen atoms are present in the combined dipeptide and tripeptide fragments after hydrolysis, considering water molecules are added to break the peptide bonds?

<p>10 (B)</p> Signup and view all the answers

Which amino acid pairing within a polypeptide would MOST likely result in electrostatic repulsion at physiological pH?

<p>Asp and Glu (D)</p> Signup and view all the answers

A segment of single-stranded DNA contains 10 base pairs, including 2 guanine and 3 adenine residues. After replication of this segment resulting in the double-stranded segment, how many thymine residues are expected in the double stranded DNA?

<p>3 (A)</p> Signup and view all the answers

Which of the following modification(s) would likely alter the overall charge of an amino acid within a protein?

<p>Phosphorylation (A)</p> Signup and view all the answers

Under which circumstance are disulfide bonds MOST likely to contribute to a protein's stability?

<p>In the endoplasmic reticulum of eukaryotic cells. (B)</p> Signup and view all the answers

How does the resonance stabilization of a peptide bond MOST directly influence protein structure?

<p>It confers partial double-bond character, restricting rotation (B)</p> Signup and view all the answers

In mass spectrometry, which property of a peptide fragment MOST directly influences its migration time through the instrument?

<p>Mass-to-charge ratio (B)</p> Signup and view all the answers

How does the formation of a glycosidic bond between two monosaccharides change their properties?

<p>It releases water as a byproduct. (B)</p> Signup and view all the answers

If an infant is lactose intolerant for a short-term, which enzyme is most likely deficient or inactive?

<p>Lactase (A)</p> Signup and view all the answers

Why is cellulose indigestible by humans, even though it is composed of glucose monomers?

<p>Humans lack the enzyme to break beta (1-&gt;4) glycosidic bonds. (B)</p> Signup and view all the answers

In a newly discovered organism, DNA analysis reveals that 20% of its bases are guanine. Considering Chargaff's rules, what percentage of the bases are expected to be thymine?

<p>30% (C)</p> Signup and view all the answers

Which factor has the MOST influence on protein separation via gel filtration chromatography?

<p>Size (D)</p> Signup and view all the answers

During differential centrifugation, which cellular component would require the HIGHEST centrifugal force to sediment?

<p>Ribosomes (A)</p> Signup and view all the answers

What is the specific function of phenyl isothiocyanate in Edman degradation during protein sequencing?

<p>Specifically labeling and removing the N-terminal residue. (B)</p> Signup and view all the answers

Which type of interaction is MOST directly responsible for stabilizing the alpha-helical structure of a protein?

<p>Hydrogen bonds between the carbonyl oxygen and amide hydrogen of the peptide backbone (C)</p> Signup and view all the answers

How does the binding of the first oxygen molecule to hemoglobin affect the affinity for subsequent oxygen molecules?

<p>It increases the affinity by inducing a conformational change. (D)</p> Signup and view all the answers

What critical structural feature is created during the formation of a phosphodiester bond in nucleic acids?

<p>A sugar-phosphate backbone with a consistent negative charge (C)</p> Signup and view all the answers

How do purines differ structurally from pyrimidines, and what is the consequence of this difference in nucleic acid structure?

<p>Purines have a double-ring structure, which occupies more space and contributes to base-stacking interactions. (B)</p> Signup and view all the answers

What is the primary structural difference between ribose and deoxyribose that leads to their distinct roles in nucleic acids?

<p>Ribose has an additional hydroxyl group at the 2' position, making it more susceptible to hydrolysis under alkaline conditions. (D)</p> Signup and view all the answers

How does the specificity of restriction enzymes contribute to recombinant DNA technology?

<p>By creating defined cleavage patterns that allow predictable insertion of DNA fragments. (A)</p> Signup and view all the answers

How would the separation pattern of DNA fragments change on an electrophoresis gel if the agarose concentration is increased?

<p>Smaller DNA fragments would be better resolved, increasing the separation between bands. (A)</p> Signup and view all the answers

Which of the following triacylglycerols would be predicted to have the highest melting point?

<p>A triacylglycerol containing three saturated C18 fatty acids (C)</p> Signup and view all the answers

Flashcards

Uracil residues in DNA segment?

There are 0 uracil residues since uracil is only found in RNA, not DNA.

Dopamine's precursor?

Dopamine is derived from the amino acid tyrosine.

GMP components?

Guanosine monophosphate (GMP) contains a nitrogenous base, a phosphate group, and a sugar (ribose).

Deoxythymidine's sugar?

Deoxythymidine contains a deoxyribose sugar.

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Peptide bonds in M-P-F-W?

The polypeptide M-P-F-W (Methionine-Proline-Phenylalanine-Tryptophan) contains 3 peptide bonds.

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Adenine residues count?

A segment of DNA containing 7 base pairs with 3 guanine residues will have 4 adenine residues.

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Amino acid side chains?

Amino acids may contain no side chains (false). All amino acids have side chains (R-groups).

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Disulfide bond partners?

Disulfide bonds are formed between cysteine (Cys) residues.

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Peptide bond proximity?

The peptide bond is physically closest to the alpha carbon.

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Mass spec identifier?

Mass spectrometry identifies amino acid sequences from the mass-to-charge ratio of gas-phase protein fragments.

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Monosaccharide linkage?

Monosaccharides are linked by glycosidic bonds.

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Lactose components?

Lactose is made of glucose and galactose.

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Cellulose makeup?

Cellulose is made of glucose and glucose.

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Purine percentage?

If a diploid organism contains 30% A residues, purines (A+G) make up 50% of its DNA.

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Gel filtration separation?

Gel filtration chromatography separates proteins based on size.

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Protein sequencing method?

Edman degradation is involved in protein sequencing.

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Alpha-helix level?

Alpha-helix is an example of protein secondary structure.

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Nucleic acid building blocks?

Constituents of nucleic acids are sugar, a phospho-diester linkage, and a base.

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Purine/pyrimidine type?

Purines and pyrimidines are bases.

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Ribose/deoxyribose type?

Ribose and deoxyribose are sugars.

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Nucleoside components?

Nucleosides contain a base and a sugar.

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Nucleotide components?

Nucleotides contain a base, a sugar, and a phosphate.

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Purine bases?

Two nucleic acid bases (purines) are Adenine (A) and Guanine (G).

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Transcription definition?

Transcription is the process of converting DNA to RNA.

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Translation definition?

Translation is the process of converting RNA to protein.

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Study Notes

  • DNA segments with 20 base pairs and 7 guanine residues contain 0 uracil residues.
  • Dopamine is derived from the amino acid Tyrosine.
  • Guanosine monophosphate contains a nitrogenous base, a phosphate, and a sugar.
  • Deoxythymidine contains deoxyribose.
  • The polypeptide M-P-F-W contains 3 peptide bonds.
  • A polypeptide with only charged polar side-chains includes Histidine (His) and Aspartic Acid (Asp).
  • A DNA segment with 7 base pairs and 3 guanine residues contains 4 adenine residues.
  • Amino acids may contain uncharged polar, charged polar, and non-polar side chains, but not "no side chains."
  • Disulfide bonds form between two Cysteine (Cys) residues.
  • A peptide bond is physically closest to the alpha carbon.
  • Mass spectrometry identifies amino acid sequences from the mass-to-charge ratio of gas-phase protein fragments.
  • Monosaccharides link to each other or to molecules via glycosidic bonds.
  • Lactose comprises glucose and galactose.
  • Cellulose comprises glucose and glucose.
  • In a diploid organism with 30% adenine residues in its DNA, 50% are purines.
  • Gel filtration chromatography separates proteins based on size.
  • During ultracentrifugation, the protein with higher density is eluted first.
  • Protein sequencing involves Edman degradation.
  • Alpha-helix exemplifies protein secondary structure.
  • The fourth oxygen molecule is the most biochemically likely to bind to hemoglobin (Hb).
  • Nucleic acids consist of a sugar, a phospho-diester linkage, and a base.
  • Purines and pyrimidines are bases.
  • Ribose and deoxyribose are sugars.
  • Nucleosides contain a base and a sugar.
  • Nucleotides contain a base, a sugar, and a phosphate.
  • Adenine (A) and Guanine (G) are purine bases.
  • Adenosine (A) and Guanosine (G) are purine nucleosides.
  • Adenylic Acid (AMP) and Guanylic Acid (GMP) are purine nucleotides.
  • Cytosine (C), Thymine (T), and Uracil (U) are pyrimidine bases.
  • Cytidine (C), Deoxythymidine (dT), and Uridine (U) are pyrimidine nucleosides.
  • Cytidylic Acid (CMP), Deoxythymidylic Acid (dTMP), and Uridylic Acid (UMP) are pyrimidine nucleotides.
  • ADP (adenosine diphosphate) and ATP (adenosine triphosphate) are well-known nucleotides.
  • DNA consists of Adenine (A), Thymine (T), Cytosine (C), and Guanine (G).
  • Deoxyribose has one less oxygen atom than ribose.
  • RNA consists of Adenine (A), Uracil (U), Cytosine (C), and Guanine (G).
  • Adenine and thymine form 2 hydrogen bonds.
  • Cytosine and guanine form 3 hydrogen bonds.
  • Transcription is the process of converting DNA to RNA.
  • Translation is the process of converting RNA to protein.
  • Nucleic acids can be cut at specific sequences by restriction enzymes.
  • Nucleic acid fragments are separated by size using electrophoresis.
  • An alpha amino acid contains an amino group (H2N), a side group (R), and a carboxyl group (COOH).
  • Amino acid side chains can be non-polar (hydrophobic), uncharged polar, or charged polar (hydrophilic).
  • Glycine (G) is a non-polar amino acid.
  • Alanine (A) is a non-polar amino acid.
  • Valine (V) is a non-polar amino acid.
  • Leucine (L) is a non-polar amino acid.
  • Isoleucine (I) is a non-polar amino acid.
  • Methionine (M) is a non-polar amino acid.
  • Proline (P) is a non-polar amino acid.
  • Phenylalanine (F) is a non-polar amino acid.
  • Tryptophan (W) is a non-polar amino acid.
  • Serine (S) is an uncharged polar amino acid.
  • Threonine (T) is an uncharged polar amino acid.
  • Asparagine (N) is an uncharged polar amino acid.
  • Glutamine (Q) is an uncharged polar amino acid.
  • Tyrosine (Y) is an uncharged polar amino acid.
  • Cysteine (C) is an uncharged polar amino acid.
  • Lysine (K) is a charged polar amino acid.
  • Arginine (R) is a charged polar amino acid.
  • Histidine (H) is a charged polar amino acid.
  • Aspartic Acid (D) is a charged polar amino acid.
  • Glutamic Acid (E) is a charged polar amino acid.
  • Cysteine can react with itself, unlike other amino acids.
  • The 20 standard amino acids share a common structure but differ in their side chains.
  • Peptide bonds link amino acid residues in a polypeptide.
  • L-Glyceraldehyde is Levorotatory, with the OH group on the left side of the alpha carbon (mainly amino acids).
  • D-Glyceraldehyde is Dextrorotatory, with the OH group on the right side of the alpha carbon (mainly carbohydrates).
  • Salting out uses solubility for protein purification.
  • Ion exchange chromatography and isoelectric focusing use ionic charge for protein purification.
  • Electrophoresis uses ion exchange for protein purification.
  • Hydrophobic interaction chromatography uses polarity for protein purification.
  • Gel filtration chromatography uses size for protein purification.
  • Affinity chromatography uses binding specificity for purification.
  • pH and temperature affect a protein's stability during purification.
  • To be sequenced, a protein must be separated into individual polypeptides that can be cleaved into sets of overlapping fragments.
  • Edman degradation removes N-terminal residues one at a time during amino acid sequencing.
  • D-Glyceraldehyde contains 3 carbons.
  • D-Ribose (Rib) contains 5 carbons.
  • D-Glucose (Glu) contains 6 carbons.
  • D-Mannose (Man) contains 6 carbons.
  • D-Galactose (Gal) contains 6 carbons.
  • Dihydroxyacetone contains 3 carbons.
  • D-Ribulose contains 5 carbons.
  • D-Fructose contains 6 carbons.
  • Aldose and Ketoses are the two smallest sugars.
  • The alpha carbon is associated with the aldehyde group.
  • The aldehyde group for aldose sugars is CHO.
  • The aldehyde group for ketose sugars is CH2OH.
  • Monosaccharides cyclize to form alpha or beta anomers.
  • Glycosidic bonds link monosaccharides to each other and to other molecules.
  • Lactose is a reducing disaccharide with galactose and glucose bonded through a beta 1, 4 bond.
  • Sucrose is a non-reducing disaccharide with glucose and fructose bonded through an alpha 1, 2 bond.
  • Beta bonds are stronger and harder to break than alpha bonds.
  • Glucose molecules in cellulose are linked by a beta (1, 4) bond.
  • N-Acetylglucosamine molecules in chitin are linked by a beta (1, 4) bond.
  • Glucose molecules in alpha-amylose are linked by an alpha (1, 4) bond.
  • There are 6 lipid groups: triacylglycerols, glycerophospholipids, sphingomyelins, gangliosides, steroids, and isoprenoids.
  • Saturated fatty acids contain single bonds.
  • Unsaturated fatty acids contain double bonds.
  • In 12:0, 12 represents the number of carbon atoms.
  • In 12:0, 0 represents the number of unsaturated bonds.
  • In 16:1n-7, n-7 represents the position of unsaturated bonds.
  • Gangliosides facilitate cell-to-cell identification.
  • Steroids contain 4 fused rings.
  • Vitamin A is a photoreceptor active in low light conditions.
  • Vitamin K participates in blood clotting.
  • Vitamin E prevents oxidative damage.
  • A lipid bilayer is made of a polar end and a non-polar end
  • Triacylglycerols refers to fatty acid esters of glycerol.
  • Glycerophospholipids refers to lipids with a glycerol backbone.
  • Isoprenoids refers to non-structural lipids with an isoprene skeleton.
  • Cortisol, testosterone, aldosterone, and beta-estradiol are the four representative steroid hormones.
  • A sphingomyelin contains a phosphocholine head group and a palmitate residue.
  • Lateral diffusion is faster than transverse diffusion in the phospholipid bilayer.
  • A fatty acid chain's physical properties are determined by length and saturation.
  • Sphingolipids resemble glycerophospholipids but may include large carbohydrate groups.

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