Protein databases with mass spectrometry analysis are not useful in proteomics studies due to the complexities of the proteome. a. All of the answers are correct. Ob. can identify proteins from small stretches of amino acid sequences Oc. Od are determined from sequence data only, never deduced from genomic data. d. None of the answers is correct.
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![Protein databases with mass spectrometry analysis
are not useful in proteomics studies due to the complexities of the proteome.
a.
All of the answers are correct.
b.
Oc.
O
can identify proteins from small stretches of amino acid sequences
are determined from sequence data only, never deduced from genomic data.
Od.
None of the answers is correct.
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- Mass spectrometry is a powerful tool in proteomics. What are the four key features of a mass spectrometer? Describe briefly how MALDI and two-dimensional polyacrylamide gel electrophoresis could be used to identify a protein expressed in cancer cells but not in normal healthy cells.Even when a gene is available and its sequence of nucleotides is known, chemical studies of the protein are still required to determine: a. molecular weight of the unmodified protein. b. the amino-terminal amino acid. c. the location of disulfide bonds. d. the number of amino acids in the protein. e. whether the protein has the amino acid methionine in its sequence.Discuss the following statement: “from the nucleotide sequence of a cDNA clone, the complete amino acid sequence of a protein can be deduced by applying the genetic code. thus, protein biochemistry has become superfluous because there is nothing more that can be learned by studying the protein.”
- Gene editing is also used to explore the structure and function ofproteins. For example, changes can be made to the coding sequenceof a gene to determine how alterations in the amino acid sequenceaffect the function of a protein. Let’s suppose that you areinterested in the functional importance of a particular glutamicacid (an amino acid) within a protein you are studying. By geneediting, you make mutant proteins in which the glutamic acidcodon has been changed to other codons. You then test the encodedmutant proteins for functionality. The results are as follows: FunctionalityNormal protein 100%Mutant proteins containingTyrosine 5%Phenylalanine 3%Aspartic acid 94%Glycine 4%From these results, what would you conclude about the…Which of the following experiments can be used to determine the localization of a protein in living cells? a. Isoelectric Focusing gel electrophoresis b. Mass spectroscopy of a MALDI-ionized protein c. X-ray Crystallography of a protein d. NMR study of a 15N-labeled protein e. Confocal microscopy study of a GFP-tagged proteinWhich of the following are common types of datalanalysis that are used in bioinformatics. O DNA sequencing O RNA sequencing Epigenomic O Proteomic QUESTION 6 Order the following processes into the correct order for the generation and analysis of sequence data v Quality control analysis v Prepare sequencing libraries v Extraction of genetic material v Sequence and generate sequence data Alignment and/or variant calling Collection of cells for analysis
- a. What are the purposes of sequence alignment? b. Define the local alignment and global alignment C. Compare local alignment and global alignment d. What is "Dot Plot" and why it is used?According to Picotti (2013), Rudi Aebersold (a leader in mass spectrometry-based proteomics) hopes that ____________ will replace Western blotting as the "go-to" approach for hypothesis-driven research about specific proteins. A. discovery proteomics B. shot-gun proteomics C. targeted proteomics D. SISCAPA E. NMRChaperones are: please explain the answer a.proteins that promote proper amino acid incorporation b.proteases that degrade improperly folded proteins c.proteins that promote proper polypeptide folding d.proteases that degrade improperly coded polypeptide chains e,proteins that promote rRNA stability
- Procedure This activity will use the Human β-hemoglobin gene, which is mutated in sickle cell anemia, with the following sequences of the first thirty (30) nucleotides: TAC CAC GTG GAC TGA GGA CAC CTC TTC AGA... 1. First transcribe the DNA sequence into the mRNA sequence. 2. Refer to the genetic code to write down the amino acid sequence that these 30 nucleotides encode beginning with the first nucleotide. 3. Generate a random number (1-30) by drawing lots in a bowl. Then locate the DNA nucleotide to "mutate" using the number drawn as the position along the gene. 4. "Roll" the tetrahedron "mutator" dice (see direction below for making the tetrahedron "mutator" dice). Note the letter on the side that is flat on the table. That is the nucleotide that will replace the nucleotide in the DNA at the position decided in the previous step. 5. Write the mutant nucleotide sequence in the row for Mutation 1, then analyze mutation. a. If it is the same nucleotide, write same nucleotide…Choose the proper order for recombinant protein purification from bacterial cells. a. lysis,pelleting by centrifugation, induction of protein expression, transformation, purification by chromatography b. induction of protein expression, transformation, pelleting by centrifugation, lysis, purification by chromatography c. transformation, induction of protein expression, pelleting by centrifugation, lysis, purification by chromatography d. purification by chromatography, lysis, pelleting by centrifugation, induction of protein expression, transformationA. Basic mechanism of 2d gel electrophoresis techniqes? B. How do we predict the protein structure from DNA sequence?
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