On the origins of tumor mutations in cancer genes: insights from the p53 gene.
Explore the source record for details and available documents.
Carcinogens↗
Biomedical subjects
G Moeckel
Publications and source records attributed to G Moeckel.
Molecular modeling information transfer with VRML: from small molecules to large systems in bioscience.
The suitability of the Virtual Reality Modeling Language (VRML) for the communication of scientists via the internet is demonstrated with recent results from computer assisted cancer research: I. Substrate channels in cytochrome P450 enzymes. II. Binding properties of the wild type and mutated p53 tumor suppressor protein. Complex 3D molecular models were used to visualize new insights in the active site access of cytochrome P450 enzymes and in the p53 protein-DNA binding achieved by the use of computational methods. These 3D models of biomolecular systems were transferred into VRML scenarios. Additional implemented features allow users to receive related information interactively. With these examples it is shown that VRML provides an efficient method for scientific information exchange by the use of complex 3D molecular models.
Binding Sites↗
Virtual reality modeling language in chemistry.
A new concept in the field of molecular modeling using the information transfer mechanism of the World Wide Web (WWW) is presented. The Virtual Reality Modeling Language (VRML) provides an object-oriented method for the description of molecular models. The structure and capabilities of this new language are introduced. It is shown that the transport of molecular models over the WWW using VRML is a very efficient and powerful method for the exchange of molecular information.
Computer Communication Networks↗
Bicarbonate-dependent betaine synthesis in rat kidney.
Explore the source record for details and available documents.
Animals↗
A new approach to analysis and display of local lipophilicity/hydrophilicity mapped on molecular surfaces.
A new method for display and analysis of lipophilic/hydrophilic properties on molecular surfaces is presented. The present approach is based on the concept of Crippen and coworkers that the overall hydrophobicity of a molecule (measured as the logarithm of the partition coefficient in an octanol/water system) can be obtained as a superposition of single atom contributions. It is also based on the concept of molecular lipophilicity potentials (MLP) first introduced by Audry and coworkers in order to establish a 3D lipophilicity potential profile in the molecular environment. Instead of using a l/r- or an exponential distance law between the atomic coordinates and a point on the molecular surface, a new distance dependency is introduced for the calculation of an MLP-value on the solvent-accessible surface of the molecule. In the present formalism the Crippen values (introduced for atoms in their characteristic structural environment) are 'projected' onto the van der Waals surface of the molecule by a special weighting procedure. This guarantees that only those atomic fragments contribute significantly to the surface values that are in the close neighbourhood of the surface point. This procedure not only works for small molecules but also allows the characterization of the surfaces of biological macromolecules by means of local lipophilicity. Lipophilic and hydrophilic domains can be recognized by visual inspection of computer-generated images or by computational procedures using fuzzy logic strategies. Local hydrophobicities on different molecular surfaces can be quantitatively compared on the basis of the present approach.
Alcohols↗
Purification of human and rat kidney aldose reductase.
In the present study we report on a rapid two-step affinity chromatographic procedure to purify aldose reductase from human and rat kidney papilla and inner medulla. This enzyme, which is responsible for sorbitol formation in the kidney, was purified 145-fold from rat and 76-fold from human kidneys by consecutive Blue Sepharose and Matrex Orange chromatography. SDS-PAGE showed a single band of 38 kD for the human enzyme and a doublet of similar molecular weight for the rat kidney aldose reductase. The enzyme was characterized by substrate specificity and kinetic constants found identical to that of other organs purified previously.
Aldehyde Reductase↗