Which amino acid sequence would yield the most optimal oligonucleotide probe? How many sequences are possible for each?
Ala-Met-Ser-Leu-Pro-Trp is having a total of 576 sequences.(4*1*6*6*4*1)
Gly-Trp-Asp-Met-His-Lys is having a total of 32 sequences.(4*1*2*1*2*2)
Arg-Ser-Met-Leu-Gln-Asn is having a total of 1864 sequences(6*6*1*6*2*2)
Cys-Val-Trp-Asn-Lys-Ile is having a total of 96 Sequences.(2*4*1*2*2*3)
From this the Arg-Ser-Met-Leu-Gln-Asn have the most optimal oligonucleotide probe with 1864 sequences and the second one is Ala-Met-Ser-Leu-Pro-Trp with 576 sequnces.
Which amino acid sequence would yield the most optimal oligonucleotide probe? How many sequences ...
2.16. Which of the following partial amino acid sequences from a protein whose gene you wish to clone would be most useful in designing an oligonucleotide probe to screen a cDNA library? (a) Met-Leu-Arg-Leu (b) Met-Trp-Cys-Trp Explain why.
How many different mRNA sequences can code for a polypeptide chain with the amino acid sequence Met - Leu - Arg? Be sure to include a stop codon. Explain your answer! 5′ ...GGAGCUCGUUGUAUU... 3′ Is this sequence RNA or DNA? How can you tell? Which amino acids are encoded, if the reading frame is as shown, starting from the correct end? What would be the effect on the amino acid sequence if the sequence were changed to 5′ GGAGACUCGUUGUAUU 3′?...
How many different amino acid sequences are possible in a polypeptide that is 10 amino acids long: Select one: a. 10^20. b. 4120. O c. 10^4. d. 20-10. THEME
While comparing the amino acid sequences of many different GPCRs, you notice the presence of conserved serine and threonine amino acids on the same cytosolic region of each receptor. You change the DNA sequence so that all of the conserved serine and threonine amino acids in the cytosolic region are converted to glutamic acid. Which of the following effects would you most likely see when cells expressing this modified GPCR are exposed to ligand compared to your control cells that...
A protein has the amino acid sequence:DSRLSKTMYSIEAPAKLDWEQNMALHow many peptide fragments would result from cleaving the sequence with....a: cyanogen bromideb: trypsinc: Which of these reagents gives the smallest single fragment (in number of amino acid residues)?Please explain how to work out this problem. Thanks!
14 Which amino acid residue sequence would mostly likely compose a transmembrane segment of a protein? (2 Points) VLVAVLESFLLLSL GRRHLGFEATFFQ GRKKRRQRRRPO NVFKGNTISDKIS 15 What would be observed if purified IgG was boiled and not reduced and then applied to SDS- PAGE (2 Points)
Describe the process by which tRNAs are charged with an amino acid. How is it possible that a specific tRNA will only be bound to a very particular amino acid, and that a different tRNA will also only be bound to a particular amino acid that is different from the first? Provide details on each component involved and of how the recognition is achieved. I am not asking for information about the energetics of the process, just about the specificity...
Which of the following would be considered the most acidic amino acid? alanine serine leucine glycine We were unable to transcribe this imageQuestion 3 2 pts When placed in water, proteins fold into discrete three dimensional shapes. Which amino acid is least likely to be found on the surface of a protein in water? lysine serine aspartic acid valine Describe how you would synthesize the dipeptide Leu-Gly. HTML Editor I EE xx, BIUA T T12pt
Which is the most inappropriate description of matured tRNA? Select one: a. 3’-end always has the CCA sequence. b. tRNA has many covalent modifications. c. Cells must carry all ~61 different tRNA to decode all possible codons in mRNA. d. Amino acid is loaded to 3’-end of tRNA. e. Amino acyl tRNA synthase for tRNATrp is specific for both Trp and the Trp anti-codon in tRNA.
A chain GIVEQCCASVCSLYQLENYCN B chain FVNQHLCGSHLVEALYLVCGERGFFYTPKA Shown above is the amino acid sequence of the hormone insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. When Sanger and colleagues began their work in 1945, it was known that insulin was a small protein consisting of two or four polypeptide chains linked by disulfide bonds. Sanger and his coworkers...