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Photo 51 is an X-ray based fiber diffraction image of a paracrystalline gel composed of DNA fiber [1] taken by Raymond Gosling, [2] [3] a postgraduate student working under the supervision of Maurice Wilkins and Rosalind Franklin at King's College London, while working in Sir John Randall's group.
The two base-pair complementary chains of the DNA molecule allow replication of the genetic instructions. The "specific pairing" is a key feature of the Watson and Crick model of DNA, the pairing of nucleotide subunits. [5] In DNA, the amount of guanine is equal to cytosine and the amount of adenine is equal to thymine. The A:T and C:G pairs ...
The first X-ray diffraction experiment was conducted in 1912 by Max von Laue, [7] while electron diffraction was first realized in 1927 in the Davisson–Germer experiment [8] and parallel work by George Paget Thomson and Alexander Reid. [9] These developed into the two main branches of crystallography, X-ray crystallography and electron ...
Other forms of elastic X-ray scattering besides single-crystal diffraction include powder diffraction, small-angle X-ray scattering and several types of X-ray fiber diffraction, which was used by Rosalind Franklin in determining the double-helix structure of DNA. In general, single-crystal X-ray diffraction offers more structural information ...
Maurice Hugh Frederick Wilkins CBE FRS (15 December 1916 – 5 October 2004) [2] was a New Zealand-born British biophysicist and Nobel laureate whose research spanned multiple areas of physics and biophysics, contributing to the scientific understanding of phosphorescence, isotope separation, optical microscopy, and X-ray diffraction.
The first high quality X-ray diffraction patterns of A-DNA were reported by Rosalind Franklin and Raymond Gosling in 1953. [1] Rosalind Franklin made the critical observation that DNA exists in two distinct forms, A and B, and produced the sharpest pictures of both through X-ray diffraction technique. [2]
Multi-wavelength anomalous diffraction (sometimes Multi-wavelength anomalous dispersion; abbreviated MAD) is a technique used in X-ray crystallography that facilitates the determination of the three-dimensional structure of biological macromolecules (e.g. DNA, drug receptors) via solution of the phase problem.
An X-ray diffraction pattern of a crystallized enzyme. The pattern of spots (reflections) and the relative strength of each spot (intensities) can be used to determine the structure of the enzyme. The relative intensities of the reflections provides information to determine the arrangement of molecules within the crystal in atomic detail.