how would you identify whether or not complete resolution of the three amino acids has been achieved
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- A mixture of amino acids that do not separate sufficiently when a single technique is used can often be separated by two-dimensional chromatography. In this technique, the mixture of amino acids is applied to a piece of filter paper and separated by chromatographic techniques. The paper is then rotated 90°, and the amino acids are further separated by electrophoresis, producing a type of chromatogram called a fingerprint. Identify the spots in the fingerprint obtained from a mixture of Ser, Glu, Leu, His, Met, and Thr.Which technique is used to identify an unknown protein ?Finally, the researcher incubates the peptide with chymotrypsin for two hours at 10 °C and analyzes the products using chromatography. Complete chymotryptic digestion of the peptide with chymotrypsin followed by chromatography yields free tyrosine and free leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio. Give the final sequence for the peptide based on the results of the acid hydrolysis, dansyl chloride reaction, and chymotryptic digestion. Use the three-letter amino acid abbreviations separated by hyphens for your answer. peptide sequence:
- You were able to extract an amino acid sequence from an unknown protein you process through mass spectrophotometry. How will you able to identify the said protein and its function?Identify if the nucleotide is GMP, CMP, AMP, UMP or TMPWestern blotting is a routine technique in protein analysis that provides qualitative and semi- quantitative data. In this work, protein separation is first carried out using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). (i) Explain the principle of SDS-PAGE in protein separation. After the electrophoretic separation, the proteins are transferred to a nitrocellulose membrane prior to staining with antibodies specific for the protein understudy. Describe in detail how the primary and secondary antibodies could aid in the protein detection process. (ii)
- Please provide a: Fischer projection of a-L-mannopyranose. and A Haworth projectionof b-D-talopyranose.Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?The OXA-M290 protein is next purified by size exclusion chromatography. To determine the best type of size exclusion resin to use, the size of OXA-M290 must first be determined. Earlier, you determined the amino acid sequence of OXA-M290 (MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASSAKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYDTKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP). Based on the amino acid sequence, what is the molecular weight of this protein? You can use the free ProtParam tool (https://web.expasy.org/protparam/) to calculate the molecular weights of proteins. Make sure to include units in your answer. Note: The amino acid sequence reported earlier does not include the His-tag that was added to OXA-M290 by the pET-28a vector. However, you do not need to consider the amino acids in the His-tag in your answer to this question. For Context ONLY: For…
- Why is it no longer considered necessary to determine the Nterminal amino acid of a protein as a separate step?are all the protein separated properly using isoelectric focusing? why or why not?You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?