Rovibrational bound states in polyatomic molecules

SIGLEAvailable from British Library Document Supply Centre-DSC:99/35620 / BLDSC - British Library Document Supply CentreGBUnited Kingdo

Fitting molecular potential energy surfaces

CCP6 is the Project Group on Heavy Particle DynamicsSIGLEAvailable from British Library Document Supply Centre- DSC:95/24685 / BLDSC - British Library Document Supply CentreGBUnited Kingdo

Wide-amplitude rovibrational bound states in polyatomic molecules

The objective of the Workshop was to bring together the leading specialists in the fields of rovibrational quantum calculation and experimental spectroscopy to share ideas and expertise on the challenging problems faced in dealing with wide-amplitude molecular motion. The results of work in this field have not only resolved difficult problems in the interpretation of high-resolution molecular spectra but have also allowed the determination of accurate potential energy surfaces (PESs) by fitting to such data. Conversely the most rigorous tests of ab initio PESs depend on being able to calculate accurate spectroscopic transitions based on the potentials for comparison with experimental dataPapers. Includes bibliographical referencesSIGLEAvailable from British Library Document Supply Centre- DSC:m03/14032 / BLDSC - British Library Document Supply CentreGBUnited Kingdo

CCDC 1581466: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures

CCDC 1581465: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures

GAP package recog: a GAP package that implements a methods for constructive recognition

This GAP package provides an implementation of methods to do group recognition using composition trees as specified in the recogbase package. This package was started and mostly developped by Max Neunhöffer and Ákos Seress, but many other people have contributed code. Everybody who contributes at least one line of code automatically becomes an author. The current list of authors is: Peter Brooksbank, Frank Celler, Stephen Howe, Maska Law, Steve Linton, Gunter Malle, Max Neunhöffer, Alice Niemeyer, Eamonn O'Brien, Colva M. Roney-Dougal and Ákos Seress. If you want or are able to contribute, please do! This package is still work in progress, in particular special code for particular leaf nodes and verification using presentations is still largely missing. However, it already provides working Monte Carlo algorithms

GAP package recog: a GAP package that implements a methods for constructive recognition

This GAP package provides an implementation of methods to do group recognition using composition trees as specified in the recogbase package. This package was started and mostly developped by Max Neunhöffer and Ákos Seress, but many other people have contributed code. Everybody who contributes at least one line of code automatically becomes an author. The current list of authors is: Peter Brooksbank, Frank Celler, Stephen Howe, Maska Law, Steve Linton, Gunter Malle, Max Neunhöffer, Alice Niemeyer, Eamonn O'Brien, Colva M. Roney-Dougal and Ákos Seress. If you want or are able to contribute, please do! This package is still work in progress, in particular special code for particular leaf nodes and verification using presentations is still largely missing. However, it already provides working Monte Carlo algorithms

Defining a Structural and Kinetic Rationale for Paralogous Copies of Phenylacetate-CoA Ligases from the Cystic Fibrosis Pathogen Burkholderia cenocepacia J2315*

The phenylacetic acid (PAA) degradation pathway is the sole aerobic route for phenylacetic acid metabolism in bacteria and facilitates degradation of environmental pollutants such as styrene and ethylbenzene. The PAA pathway also is implicated in promoting Burkholderia cenocepacia infections in cystic fibrosis patients. Intriguingly, the first enzyme in the PAA pathway is present in two copies (paaK1 and paaK2), yet each subsequent enzyme is present in only a single copy. Furthermore, sequence divergence indicates that PaaK1 and PaaK2 form a unique subgroup within the adenylate-forming enzyme (AFE) superfamily. To establish a biochemical rationale for the existence of the PaaK paralogs in B. cenocepacia, we present high resolution x-ray crystal structures of a selenomethionine derivative of PaaK1 in complex with ATP and adenylated phenylacetate intermediate complexes of PaaK1 and PaaK2 in distinct conformations. Structural analysis reveals a novel N-terminal microdomain that may serve to recruit subsequent PAA enzymes, whereas a bifunctional role is proposed for the P-loop in stabilizing the C-terminal domain in conformation 2. The potential for different kinetic profiles was suggested by a structurally divergent extension of the aryl substrate pocket in PaaK1 relative to PaaK2. Functional characterization confirmed this prediction, with PaaK1 possessing a lower Km for phenylacetic acid and better able to accommodate 3′ and 4′ substitutions on the phenyl ring. Collectively, these results offer detailed insight into the reaction mechanism of a novel subgroup of the AFE superfamily and provide a clear biochemical rationale for the presence of paralogous copies of PaaK of B. cenocepacia

Structural basis for conserved complement factor-like function in the antimalarial protein TEP1

Thioester-containing proteins (TEPs) are a major component of the innate immune response of insects to invasion by bacteria and protozoa. TEPs form a distinct clade of a superfamily that includes the pan-protease inhibitors α2-macroglobulins and vertebrate complement factors. The essential feature of these proteins is a sequestered thioester bond that, after cleavage in a protease-sensitive region of the protein, is activated and covalently binds to its target. Recently, TEP1 from the malarial vector Anopheles gambiae was shown to mediate recognition and killing of ookinetes from the malarial parasite Plasmodium berghei, a model for the human malarial parasite Plasmodium falciparum. Here, we present the crystal structure of the TEP1 isoform TEP1r. Although the overall protein fold of TEP1r resembles that of complement factor C3, the TEP1r domains are repositioned to stabilize the inactive conformation of the molecule (containing an intact thioester) in the absence of the anaphylotoxin domain, a central component of complement factors. The structure of TEP1r provides a molecular basis for the differences between TEP1 alleles TEP1r and TEP1s, which correlate with resistance of A. gambiae to infection by P. berghei