Visualising proteins: Difference between revisions
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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]]). | 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|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|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 is one of the most basic techniques used in determining the strutures of biological molecules like proteins<ref>William Reusch. 2003. Nuclear Magnetic Resonance Spectroscopy. [ONLINE] Available at: http://www2.chemistry.msu.edu/faculty/reusch/VirtTxtJml/Spectrpy/nmr/nmr1.htm. [Accessed 16 October 14].</ref>. This is done through measuring the many short proton-proton distances and angles and restraining the protein structure with these computationally<ref>NMR of Proteins. [ONLINE] Available at: http://www.nmr2.buffalo.edu/resources/edu/matr/nmr2_2004.pdf. [Accessed 16 October 14].</ref>. <br> | *NMR is one of the most basic techniques used in determining the strutures of biological molecules like proteins<ref>William Reusch. 2003. Nuclear Magnetic Resonance Spectroscopy. [ONLINE] Available at: http://www2.chemistry.msu.edu/faculty/reusch/VirtTxtJml/Spectrpy/nmr/nmr1.htm. [Accessed 16 October 14].</ref>. This is done through measuring the many short proton-proton distances and angles and restraining the protein structure with these computationally<ref>NMR of Proteins. [ONLINE] Available at: http://www.nmr2.buffalo.edu/resources/edu/matr/nmr2_2004.pdf. [Accessed 16 October 14].</ref>. <br> | ||
*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. | *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.<br> | ||
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=== References: === | === References: === | ||
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Revision as of 00:21, 24 October 2014
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 is one of the most basic techniques used in determining the strutures of biological molecules like proteins[1]. This is done through measuring the many short proton-proton distances and angles and restraining the protein structure with these computationally[2].
- 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.
References:
- ↑ William Reusch. 2003. Nuclear Magnetic Resonance Spectroscopy. [ONLINE] Available at: http://www2.chemistry.msu.edu/faculty/reusch/VirtTxtJml/Spectrpy/nmr/nmr1.htm. [Accessed 16 October 14].
- ↑ NMR of Proteins. [ONLINE] Available at: http://www.nmr2.buffalo.edu/resources/edu/matr/nmr2_2004.pdf. [Accessed 16 October 14].