Research on Protein Structure Determination

Structure determination in crystallography refers to the process of elaborating the three-dimensional positional coordinates and also, usually, the three-dimensional anisotropic displacement parameters of the scattering centres in an ordered crystal lattice. Where a crystal is composed of a molecular compound, the term generally includes the three-dimensional description of the chemical structures of each molecular compound present. Most structure determination techniques involve the diffraction of electromagnetic or matter waves of wavelengths comparable to atomic dimensions. Bragg's law specifies the condition for plane waves to be diffracted from lattice planes. The diffracted radiation passing through a crystal emerges with intensity varying as a function of scattering angle. This variation arises from constructive and destructive interference of scattered beams from the planes associated with the different atoms present in the lattice. The result is seen by an imaging detector as a pattern of diffraction spots or rings. Some important diffraction-based techniques are single-crystal X-ray diffraction, X-ray powder diffraction, X-ray fibre diffraction, neutron powder diffraction, neutron single-crystal diffraction Other techniques for three-dimensional structure determination that are complementary to diffraction methods include electron microscopy & nuclear magnetic resonance spectroscopy. Journal of Biocatalysis & Biotransformation emerges as a best indexed, hybrid journal with impact factor compared to other competitive journals focusing on Biochemistry, its classifications like protein binding assay, binding affinity, Protein structure determination by bringing up the recent research to global scientific community through its publications. The papers submitted are undergone through perfect plagiarism checks, later peer reviewed by the expert group and published after through revisions.