lecture6_9_18_08 - ime-o f-f light mass spectrometry ESI :...

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Overview: protein methods Homework: 3.1, 3.4, 3.7, 3.10, 3.11, 3.12 Lecture 6 Chapter 3: Stryer Read Ch 3: focus on 1) 3.1 Purification of proteins 2) 3.2 Sequence determination 3) 3.5 Mass spectrometry 4) 3.6 Protein structure Protein isolation from cells desalting gel-filtration chromatography ion-exchange chromatography affinity chromatography HPLC/FPLC
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Gel electrophoresis: SDS PAGE Gel electrophoresis: SDS PAGE Determining protein sequences Ala-Gly-Asp-Phe-Arg-Gly amino acids 6 M HCl ! , 100 °C 24 h Determination of amino acid composition
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Determining protein sequences Cleavage by CNBr Cleavage by trypsin
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Overlap of peptides: establishing the correct order Disulfide-bond reduction Overlap of peptides: establishing the correct order
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Verifying protein identity MALDI-TOF : m atrix-a ssisted l aser d esorption- i onization t
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Unformatted text preview: ime-o f-f light mass spectrometry ESI : e lectrospray i onization m ass spectrometry MALDI-TOF MALDI-TOF mass spectrum Proteomics: analysis of peptide fragments by mass spectrometry Solving the protein structure X-ray crystallography experiment to determine the three-dimensional protein structure at atomic resolution Electron density map Resolution is important! Protein structure determination in solution NMR : n uclear m agnetic r esonance Protein structure determination by NMR Two- or three-dimensional NMR techniques are necessary to solve the structures of proteins NOESY : n uclear O verhauser e nhancement s pectroscopy NOESY : n uclear O verhauser e nhancement s pectroscopy Structures calculated on the basis of NMR constraints...
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This note was uploaded on 08/04/2010 for the course CHM 6620 taught by Professor Dr.christinechow during the Fall '08 term at Wayne State University.

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lecture6_9_18_08 - ime-o f-f light mass spectrometry ESI :...

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