Construction of a preliminary three-dimensional structure of angiogenin

The method of Computer modeling was used to build the three-dimensional structure of Angiogenin, based on its homology to bovine pancreatic ribonuclease A, the X-ray crystal structure of which is known. The positions of the catalytically important residues His-13, Lys-40, and His-114 were considered. The fit of the backbone of angiogenin to that of bovine pancreatic ribonuclease A (bpr) was then optimized by taking account of residue deletions. The X-ray structure of bovine pancreatic ribonuclease A with the bound inhibitor, (3–5)Cytidinephosphorylguanosine (CpG) was used as a template to fit the active site of angiogenin. Finally the model of angiogenin was energy minimized under a single layer of explicit water molecules representing the first solvation shell.     

High spin spectroscopy of 139Pr

The high spin states in N=80 ¹³⁹Pr have been investigated by in-beam γ-spectroscopic techniques following the reaction ¹³⁰Te (¹⁴N, 5n) reaction at E=75 MeV, using a gamma detector array, consisting of seven 23% compton-suppressed high purity germanium detectors and a multiplicity ball of fourteen bismuth germanate elements. Based on γ-γ coincidence data, the level scheme of ¹³⁹Pr has been considerably extended up to 7.2 MeV excitation. Tentative spin-parity assignments are done for the newly proposed levels on the basis of the DCO ratios corresponding to strong gates and the available information from the earlier light ion experiments.     

Antagonist binding in the rat muscarinic receptor A study by docking and X-ray crystallography

A series of agonists to the rat muscarinic receptor have been docked computationally to the active site of a homology model of rat M1 muscarinic receptor. The agonists were modelled on the X-ray crystal structure of atropine, which is reported here and the docking studies are shown to reproduce correctly the order of experimental binding affinities for the agonists as well as indicate where there appear to be inconsistencies in the experimental data. The crystal and molecular structure of atropine (tropine tropate; -[hydroxymethyl]benzeneacetic acid 8-methyl[3.2.1]oct-3-yl ester C₁₇H₂₃NO₃) has been determined by X-ray crystallography using an automated Patterson search method, and refined by full-matrix least-squares to a final R of 0.0452 for 2701 independent observed reflections and 192 parameters using Mo K radiation, λ = 0.71073 Å at 150 K. The compound crystallises in space group Fdd2 with Z = 16 molecules per unit cell.     

Level structures of 95,97Mo — A comparative study

High-spin states of ^95,97Mo (Z=42, N=53,55) nuclei have been investigated through ⁸²Se(¹⁸O, xn) reaction at Eb=60 MeV. The level scheme in ⁹⁵Mo has been observed upto ≏ 10 MeV in the present experiment. The level structure shows mainly single particle character. In ⁹⁷Mo, the ground state level sequence has been extended to ≏ 4.5 MeV while the previous information had been up to 2.4 MeV. A negative parity band built on 1437 keV (11/2⁻) excited state has been extended to 5.5 MeV. The structure seems to show a coexistence of single particle and collective modes of excitation. Properties of both the nuclei have been compared with shell model calculations using OXBASH.     

High spin rotational bands in 65Zn

The nucleus ₃₀ ⁶⁵ Zn was studied using the ⁵²Cr(¹⁶O, 2pn)⁶⁵Zn reaction at a beam energy of 65 MeV. The level scheme is extended up to an excitation energy of 10.57 MeV for spin-parity (41/2?) with several newly observed transitions placed in it.     

A comparative study of the single crystal X-ray determination and molecular modelling of the binding of oligomycin to ATP Synthase

Recently published X-ray structures of three common forms, A, B and C, of oligomycin, including absolute configurations, are investigated to examine their binding to ATP Synthase. The X-ray studies reveal regions with differences in three-dimensional structure and hydrogen bonding propensity between the oligomycins, which may be associated with their potential to bind to sites on ATP Synthase. Computational docking studies carried out using MOE with the X-ray structures and an homology model of the F_O domain of ATP Synthase from Escherichia coli, are used to derive an induced fit pocket. Docking of all oligomycins to this pocket indicate that the B and C forms bind more tightly than the A form. Consideration of the single crystal X-ray data alone indicate the B form may be the best inhibitor and that O(24) is the most important ligating group for binding, this is supported by the docking data. The latter reveals Asn214 and other key proton translocating residues to be the main residues contacted by the inhibitor. These data allow the binding modes of different forms of oligomycin to be deduced from X-ray single crystal data supported by molecular modelling and computational docking studies.