Difference between revisions of "Proteomics-OG"

Latest revision as of 11:13, 19 June 2016

What is proteome? the entire set of proteins expressed by a genome, cell tissue, or organism at a certain time.

Type

proteomics : study of proteome

How to study the proteome

separation >> gel electrophoresis
- isoelectric focusing (charge) + SDS-PAGE (molecular weight) --> gel dyed with comassie blue to visualization
How to know their identity (their component, amino acids sequence ) >> mass spectroscopy
- Peptide mass fingerprinting : cleave the protein into short peptides --> deduce the protein's identity based on sequence database
- Tandem mass spectrometry : isolate individual peptides --> collide them with non-reactive gas --> cataloguing the [fragment ion] produced (by detecting ion, they can deduce the identity of peptides)

methods

cryo-electron microscopy
- what ? TEM studied at cryogenic temperature
- advantage : do not require crystallization / relatively easy
- disadvantage : low resolution
microscopy
- source: reflection , diffraction of electromagnetic radiation beams interacting with the specimen
- Types : TEM / SEM
- disadvantage : limitation of resolution / show specimen by only dark or light color
NMR
- source : nuclear magnetic resonance. It means that electromagnetic radiation that nuclei absorb and re-emit. this radiaction is in the state of specific resonance frequency
- frequency is directly proportional to the strength of the magnetic field
- type
  - Solid-state NMR spectroscopy
  - Multi-dimensional NMR spectroscopy
  - Fourier-transform spectroscopy
  - CW spectroscopy

protein structure

Post translational modifications

experimental methods >> identifying proteins

Interaction proteomics

reference

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 	</li>
 </ul>
+<p>&nbsp;</p>
+<hr />
+<p>reference</p>
+<p>1)&nbsp;https://en.wikipedia.org/wiki/Proteomics</p>
+<p>2)&nbsp;http://www.slideshare.net/COST-events/proteomics-analysis-basics-and-applications</p>