Visualising proteins: Difference between revisions
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Atomic level structures of proteins are visualised by x-ray crystallography, NMR (nuclear magnetic resonance), EM (electron microscopy) or SPA (single particle analysis). | Atomic level structures of proteins are visualised by [[x-ray crystallography|x-ray crystallography]], NMR ([[nuclear magnetic resonance|nuclear magnetic resonance]]), EM ([[electron microscopy|electron microscopy]]) or SPA ([[single particle analysis|single particle analysis]]). | ||
*X- ray crystallography requires the growth of protein crystals, which is relavitely simple. It requires diffraction to be measured from the protein crystal. Information is produced in a series of black dots, which are reflections, to form the basis of structure solution. Eventually this comes together to form a 3D image. | *X- ray crystallography requires the growth of [[protein crystals|protein crystals]], which is relavitely simple. It requires diffraction to be measured from the protein crystal. Information is produced in a series of black dots, which are reflections, to form the basis of structure solution. Eventually this comes together to form a 3D image. | ||
*NMR studies proteins in solution but is limited to only small medium proteins. | *NMR studies proteins in solution but is limited to only small medium proteins. | ||
*EM/SPA are more suited to large protein complexes and viruses. EM uses magnetic coils to focus a beam of electrons on the specimen. The sample in the EM must be kept in a vacuum. This has more penetrating power than light microscopy. SPA involves taking many images of a sample frozen in water in random orientations. These 2D images can then be combined to provide a 3D view of the protein. | *EM/SPA are more suited to large protein complexes and [[Virus|viruses]]. EM uses magnetic coils to focus a beam of electrons on the specimen. The sample in the EM must be kept in a vacuum. This has more penetrating power than light microscopy. SPA involves taking many images of a sample frozen in water in random orientations. These 2D images can then be combined to provide a 3D view of the protein. | ||
The equiptment used to carry out such techniques is very expensive. | The equiptment used to carry out such techniques is very expensive. | ||
Revision as of 20:19, 24 October 2012
Atomic level structures of proteins are visualised by x-ray crystallography, NMR (nuclear magnetic resonance), EM (electron microscopy) or SPA (single particle analysis).
- X- ray crystallography requires the growth of protein crystals, which is relavitely simple. It requires diffraction to be measured from the protein crystal. Information is produced in a series of black dots, which are reflections, to form the basis of structure solution. Eventually this comes together to form a 3D image.
- NMR studies proteins in solution but is limited to only small medium proteins.
- EM/SPA are more suited to large protein complexes and viruses. EM uses magnetic coils to focus a beam of electrons on the specimen. The sample in the EM must be kept in a vacuum. This has more penetrating power than light microscopy. SPA involves taking many images of a sample frozen in water in random orientations. These 2D images can then be combined to provide a 3D view of the protein.
The equiptment used to carry out such techniques is very expensive.