Which of the following technique/s can be used to determine the amino acid sequence of a polypeptide ? O1.chemical sequencing + physical fragmentation O2. physical fragmentation 0 3. chemical sequencing 04.X-ray crystallography O5. NMR 0 6. NMR + X-ray crystallography

Which of the following technique/s can be used to determine the amino acid sequence of a polypeptide ? O1.chemical sequencing + physical fragmentation O2. physical fragmentation 0 3. chemical sequencing 04.X-ray crystallography O5. NMR 0 6. NMR + X-ray crystallography

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.69P

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The image below is a positive ionization mode Electrospray ionization-mass spectrum (ESI-MS) spectrum for a peptide, obtained using high resolution mass spectrometry. If ionization occurs through de-protonation (assuming that the mass of a proton is 1.0 Da), what is the neutral mass of the peptide, in Da? 627.271 627.604 100 - 627.938 628.271 628.604 628.938 627.0 628.0 629.0 mass/charge (m/z) 628.271 626.271 1878.813 O 1884.813 % Abundance
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Chemistry a. Are there methods other than spectrophotometry to determine protein concentration? If there is, please provide an explanation of this method along with its advantages and disadvantages! b. Explain the principle of protein separation by electrophoresis method! c. Can protein electrophoresis method be used to characterize proteins? Please explain why!
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About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.
What are two ways to measure the total amount of all proteins in a purification sample? O 1) Calculating the yield and 2) calculating the purity of a purification. O 1) Measuring absorbance at 280 nm and 2) using an enzymatic assay for your protein of interest. O 1) Quantitating the amount of your protein of interest using binding of a labeled antibody (e.g.. an ELISA) and 2) using a dye-binding assay. O 1) Measuring absorbance at 280 nm and 2) using a dye-binding assay.
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