A B Figure 1. (A and B) Crystal structures of HAstV-1 P2 spike domain. (A) Dimers of HAstV-1 P2 spike domain with a rotation of 180 degrees along the y-axis from each other. (B) Rotation of 90 degrees along the x-axis is shown with black arrows.
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determine the structure of p2 spike. is it primary, secondary, tertiary, or quaternary?
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- 3 of 3 A protein was completely digested with trypsin and an internal peptide (i.e. not derived from the N- or C-terminals) was purified. Determine its sequence from the following information: a) amino acid analysis yields one mole of D, T, P, L, Y, F, K, and R per mole of peptide; b) treatment of the intact peptide with FDNB, followed by acid hydrolysis, gives DNP-L and &-DNP-K; c) treatment of the intact peptide with chymotrypsin yields a tripeptide containing K, T, and D; a tetrapeptide containing P, L, F, and R, and free tyrosine; d) the tripeptide, in part c, yields DNP-T and ɛ-DNP-K after reaction with FDNB and acid hydrolysis. Note: trypsin will not cleave on the carboxyl side of arginine or lysine if the next amino acid (donating the amino group) is proline. Put your answer here:.A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from addingA heptapeptide was found to have an amino acid composition of Asp, Leu, Lys, 2 Met, Phe and Tyr. (a) Trypsin has no effect on the heptapeptide. (b) The phenyl thiohydantoin released by Edman degradation revealed phenylalanine in the N-terminus. (c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. (d) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide? Answer Format: (Three letter abbreviation with dash ie., Ala-Gly-…) *
- During SDS-PAGE, glycoproteins migrate as relatively diffuse bands, whereas nonglycosylated proteins typically migrate as narrow, well-defined bands. Explain the reason for this difference in electrophoretic behavior.The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group of serine, threonine, or tyrosine residues. The R-group for phosphoserine is shown at right. A) The image below is an Isoelectric focusing strip that shows the unphosphorylated protein-of-interest (in blue). To which side of the unphosphorylated protein would you expect to see the phosphorylated protein? (Draw an arrow to indicate direction). Briefly justify your answer. un-phosphorylatable: Low pH Justify: B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr to appear as though it is always phosphorylated or never phosphorylated at a particular site. What amino acid substitution should you use to preserve similar dimensions as Ser (or Thr) but make the side chain appear to be: constitutively (always) phosphorylated: Justify: Ser or Thr → O O=P-O O I CH₂ Ser or Thr➜ Phosphoserine High pH
- = A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [F] = ab M21. Which protein structure is most consistent for the hydropathy graph of the intrinsic membrane protein shown below? +168 F +84 -84 -168 20 100 200 300 First amino acid in window A) A seven-helix serpentine receptor B) A Type I integral membrane protein C) A Type Il integral membrane protein D) A GPI-anchored protein E) A beta-barrel protein with about 10 membrane-spanning strands. Hydropathy index (kJ mol-1)One of the amino acid sequences in the lysozyme protein from the bacterial virus T4 studiesby Streisinger and co-worker was .... Lys – ser – pro – ser – leu – asn – ala – ala – lys. Thisparticular amino acid was found to have changed to lys – val – his –his –leu –met –ala –ala–lys... as a result of a single nucleotide deletion and addition approximately 15 bases apartin the mRNA. Which base was deleted and which was added? Give the altered sequence of bases inthe altered amino acid.
- One of the amino acid sequences in the lysozyme protein from the bacterial virus T4 studiesby Streisinger and co-worker was .... Lys – ser – pro – ser – leu – asn – ala – ala – lys. Thisparticular amino acid was found to have changed to lys – val – his –his –leu –met –ala –ala–lys... as a result of a single nucleotide deletion and addition approximately 15 bases apartin the mRNA.a. What is the sequence of the nucleotides that produce the original protein.b. Which base was deleted and which was added? Give the altered sequence of bases inthe altered amino acid.Bacteriorhodopsin is an integral membrane protein containing 248 amino acids. X- ray analysis of this protein reveals that it consists of seven parallel a-helical segments, each of which traverses the bacterial cell membrane. Calculate the minimum number of amino acid residues necessary for a single a-helical segment to completely traverse the bacterial cell membrane (assume the membrane has a thickness of 4.1 nm). (a) (b) Estimate the fraction of the bacteriorhodopsin protein that is involved in membrane-spanning helices.Each type of molecule listed below is recognized by a specific class of nuclear import receptor (importin) or nuclear export receptor (exportin). For each type of molecule, state whether you think it is recognized by an importin or exportin and explain why (in terms of where that molecule is synthesized, what that molecule does, and where it does it). (a) RNA polyermase II: (b) ribosomal protein: (iii) †RNA: