![Biochemistry](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_largeCoverImage.gif)
Concept explainers
REFLECT AND APPLY Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins.
(a) What level is shown by double-stranded DNA?
(b) What level is shown by tRNA?
(c) What level is shown by mRNA?
![Check Mark](/static/check-mark.png)
Interpretation:
Corresponding to the different levels of protein structure, the structural level existing in the given three nucleic acid molecules is to be determined.
Concept introduction:
Proteins are polymers of amino acids that are composed of one or more polypeptide chains. Several amino acids are linked to each other via a peptide bond to form a polypeptide chain. The structure of a protein is thus dependent on the degree of complexity of the polypeptide chains.
Based on the complexity of the polypeptide chains, protein structures can be classified as primary, secondary, tertiary, and quaternary. The primary structure is the simplest structure and describes the linear arrangement of amino acids to form a polypeptide chain. Folding of the polypeptide chains due to interactions between atoms of the backbone form the secondary structure.
Further folding due to the interactions between the R groups of amino acids to form a 3D structure of a protein is referred to as the tertiary structure. Presence of two or more polypeptide chains (subunits) in a 3D conformation within a single protein comprises the quaternary structure.
Answer to Problem 1RE
Solution:
a) Secondary structure
b) Tertiary structure
c) Primary structure
Explanation of Solution
a) The level of double-stranded DNA.
Double-stranded DNA is composed of two strands of opposite polarity that are twisted around each other. The backbone of these strands is made up of alternating deoxyribose and phosphate groups and each deoxyribose is linked with one of the four bases: adenine (A), cytosine (C), guanine (G), or thymine (T). The bonds formed between the bases (A-T and G=C) is responsible for the two strands of the double-stranded DNA being held together.
In the secondary structure of proteins, the polypeptide chains fold and are held together by the interactions between the atoms of the backbone. Similarly, in double-stranded DNA, the two strands are held together by the interaction between bases present on the two strands.
Therefore, double-stranded DNA is considered to have a secondary structure.
b) The level of tRNA.
Transfer RNA, as the name suggests, acts as an adaptor molecule that transfer the amino acid residues to the growing polypeptide chain during the process of translation. tRNA can have a primary structure, clover-shaped secondary structure, or a 3D L-shaped tertiary structure. The L-shaped structure of tRNA is bonded and stabilized by the base pairing between nucleotides in the D loop and the TΨC loop.
During the process of translation, the tertiary structure of the tRNA plays a major role as it fits into the P and A sites of the ribosome and allows the addition of amino acids to the growing polypeptide chain.
Therefore, tRNA is considered to have a tertiary structure.
c) The level of mRNA.
Messenger RNA is the chief RNA molecule that acts as a messenger to transfer the genetic information stored in the DNA to the ribosomes to generate the corresponding protein sequences. mRNA is generated from the nucleotide sequences which are complementary to the template strand of DNA during the process of transcription.
mRNA is single-stranded and also lacks any major folding or secondary structures.
Therefore, mRNA is considered to have a primary structure.
Want to see more full solutions like this?
Chapter 9 Solutions
Biochemistry
- Kranse et. al. measured the temperature dependence of conductance using membranescontaining the phospholipids glyceryl dipalmitate and glyceryl distearate. Describe themodifications in membrane content that you would employ to: (a) shift the temperature of the phase transition (b) make the ion conductance curve for valinomycin andnonactin more like that of gramicidinarrow_forwardObtain the sequence for the 5-HT receptor HTR1A and generate a hydropathy plot usingthe ExPASY tool ProtScale, the appropriate window, and the Kyte-Doolittle weightingalgorithm. How many transmembrane domains are present in this receptor? Attach yourhydropathy plot to your assignment.arrow_forwardCompare and contrast the structural features of the ion carrier valinomycin with those of achannel former like gramicidin. How does structural information help explain the mechanismby which these molecules conduct ions across membranes?arrow_forward
- A typical integral membrane protein has a stretch (or stretches) of ~20 hydrophobic aminoacids that form an α-helix that spans the bilayer (as is found in membrane proteins such asglycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural features of gramicidin with a membrane-spanning α-helix. Explain how gramicidin can forman ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).arrow_forwardThe titration curve of alanine shows the ionization of two functional groups with pK values of 2.34 and 9.69, corresponding to the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of alanine also shows the ionization of only two functional groups, although the experimental pK values are different. The table summarizes the trend in pK values. Amino acid or peptide Ala Ala-Ala pKj pk₂ 2.34 9.69 3.12 8.30 Ala-Ala-Ala 3.39 8.03 Ala-(Ala)-Ala, n ≥ 4 3.42 7.94 Modify the molecules to show the oligopeptide Ala-Ala-Ala. You can modify the molecules by moving, adding, deleting, or changing atoms, bonds, or charges. C Select c Draw Templates More H с N 0 S Cl H H | | || H CH3 H CH, H CH₂ Complete the statements about the the pK, values of the Ala-Ala-Ala oligopeptide. The pK₁ value of 3.39 is associated with the -COO group of Ala-Ala-Ala. The pK2 value of 8.03 is associated with the -NH group of Ala-Ala-Ala. Erase Q2 Q…arrow_forwardFacts from the bacterium mals and to dept kan apa in a peptide with antidic properties. This peptide complex with the call membrance of other hacterial species, leading in bacterial death The structure of the peptide has been determined from (a) Cmplete acid hydes of the peptide, followed by amino acid analys, yielded quiar anunt of Lan, Om, Pfx, Prxa, and Wall Cmtiti, an amino acid od prosentin pockets but present in some peptides. Com has the tracture H *H,N-CH-CH-CH, -C- COO (b) The weight of the peptide in approximately 1,200 Th (c) The peptide failed to undergo hydrolysis when treated with the Hydrolysis of the carbonyl-terminal residue of a polypeptide une "NH, the year. This call there Pro or the police does not contain a froz (d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and ched only from and the derivative NO, Н ON NHCHI CH, CH, C coo +NH, (Hint: The 2,4-diphenyl derivative involves the amino group of a side chain rather than the…arrow_forward
- Electrophoresis Macmillan Learning Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and lane 2 contains chymotrypsin pre-treated with performic acid. 1 2 Why does performic acid treatment of chymotrypsin generate three bands in lane 2? ° Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues. The three peptides are impurities in the original chymotrypsin sample. Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues. Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin. Correct Answerarrow_forwardExtracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death. The structure of the peptide has been determined from a series of observations. (a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure H 'H,N-CH, - CH2 CH2 CH2 - C - COO- NH, (b) The molecular weight of the peptide is approximately 1,200 Da. (c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free carboxyl group. (d) Treatment of the intact peptide with…arrow_forwardAt a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pl is zwitterionic. CH3 H,N CH3 ** H¸N-C H Zwitterionic H Uncharged OH Select statements that explain why alanine is predominantly zwitterionic at its pl. pk of alanine's amino group is more than its pl. pk of alanine's carboxyl group is more than its pl. PK of alanine's carboxyl group is less than its pl. pk of alanine's amino group is less than its pl. Correct Answer What fraction of alanine is in the completely uncharged form at its pl? 1 in 2.2 × 107 1 in 1.6 × 10² 1 in 4680 1 in 9460arrow_forward
- How does a voltage-gated sodium channel work? Specifically, how and why does a change in voltage trigger their opening? Please be detailedarrow_forwardWhen sodium ions enter a neuron during depolarization, they trigger the opening of additional voltage-gated sodium channels nearby, creating a positive feedback loop where the influx of sodium ions further depolarizes the membrane, causing even more sodium channels to open and allowing more sodium ions to enter the cell, thus sustaining the depolarization process until the action potential peaks. But how and why exactly does the influx of sodium ions trigger more sodium channels to let in more sodium? Please explainarrow_forwardDraw the chemical structure of the tripeptide, HEL (L - amino acids), at pH = 7.0. Calculate isoelectric pointarrow_forward
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305961135/9781305961135_smallCoverImage.gif)