Cheminfo Retrieval Class Six FA09

submitted by: jcbradley
This is the lecture from the sixth Chemical Information Retrieval class at Drexel University on October 29, 2009. It starts with a review of some of the new questions answered by students from the chemistry publishing FAQ, which covers patent information and accessing electronic journals at Drexel. Tony Williams submitted a puzzle to resolve conflicting structures in ChemSpider, which is too difficult to be a regular assignment. It requires re-analyzing spectroscopic data in papers where...

Translational Proteomics 2.0 Meeting: SEQUEST and TPP Tips

submitted by: dachian

Advanced tips on using SEQUEST and TPP by Jimmy Eng of U. of Washington, the co-inventor of SEQUEST

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

linked profile(s): Lei Wang
submitted by: apryl
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized β-sheet–rich aggregates, termed amyloid-like fibrils. Amyloid fibrils are associated with several...
Authors: David Eisenberg, Samir K Maji, Roland Riek, Michael R Sawaya, Lei Wang

Antibody-protein interactions: benchmark datasets and prediction tools evaluation

linked profile(s): juliap
submitted by: apryl
Background The ability to predict antibody binding sites (aka antigenic determinants or B-cell epitopes) for a given protein is a precursor to new vaccine design and diagnostics. Among the various methods of B-cell epitope identification X-ray crystallography is one of the most reliable methods. Using these experimental data computational methods exist for B-cell epitope prediction. As the number of structures of antibody-protein complexes grows, further interest in prediction...
Authors: Julia v Ponomarenko, Philip e Bourne

Structural analysis of the evolution of steroid specificity in the mineralocorticoid and glucocorticoid receptors

submitted by: Michael Baker
Background The glucocorticoid receptor (GR) and mineralocorticoid receptor (MR) evolved from a common ancestor. Still not completely understood is how specificity for glucocorticoids (e.g. cortisol) and mineralocorticoids (e.g. aldosterone) evolved in these receptors. Results Our analysis of several vertebrate GRs and MRs in the context of 3D structures of human GR and MR indicates that with the exception of skate GR, a cartilaginous fish, there is a...
Authors: Michael e Baker, Charlie Chandsawangbhuwana, Noah Ollikainen

Multipolar representation of protein structure

linked profile(s): Phil
submitted by: jmath
Background That the structure determines the function of proteins is a central paradigm in biology. However, protein functions are more directly related to cooperative effects at the residue and multi-residue scales. As such, current representations based on atomic coordinates can be considered inadequate. Bridging the gap between atomic-level structure and overall protein-level functionality requires parameterizations of the protein structure (and other...
Authors: Apostol Gramada, Philip e Bourne

Wiggle—Predicting Functionally Flexible Regions from Primary Sequence

submitted by: jgu
The Wiggle series are support vector machine–based predictors that identify regions of functional flexibility using only protein sequence information. Functionally flexible regions are defined as regions that can adopt different conformational states and are assumed to be necessary for bioactivity. Many advances have been made in understanding the relationship between protein sequence and structure. This work contributes to those efforts by making strides to understand the relationship...
Authors: Jenny Gu, Michael Gribskov, Philip E Bourne

Structural Evolution of the Protein Kinase–Like Superfamily

linked profile(s): Phil
submitted by: escheeff
The protein kinase family is large and important, but it is only one family in a larger superfamily of homologous kinases that phosphorylate a variety of substrates and play important roles in all three superkingdoms of life. We used a carefully constructed structural alignment of selected kinases as the basis for a study of the structural evolution of the protein kinase–like superfamily. The comparison of structures revealed a “universal core” domain consisting only of...
Authors: Eric d Scheeff, Philip e Bourne