sequence analysis, protein

Large-scale Phosphorylation Analysis (Proteomics): Dr. Sean Beausoleil, Harvard

submitted by: dachian

Analyzing phosphopeptides using proteomics mass spectrometry is challenging, especially for large-scale data sets. The problem and solution is discussed by Dr. Sean Beausoleil (Harvard Medical School), who is the co-inventor of the ASCORE algorithm for phosphorylation site localization.

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...

Bookcast - Structural Bioinformatics 2nd Edition Gu & Bourne (Eds.)

submitted by: Phil
Further details of the book can be found at http://eu.wiley.com/WileyCDA/WileyTitle/productCd-0470181052.html and on Google Books http://books.google.com/books?id=4H_ai7ivRIcC&pg=PP1&dq=structural+bioin... .

The R403Q Myosin Mutation Implicated in Familial Hypertrophic Cardiomyopathy Causes Disorder at the Actomyosin Interface

submitted by: apryl
Background Mutations in virtually all of the proteins comprising the cardiac muscle sarcomere have been implicated in causing Familial Hypertrophic Cardiomyopathy (FHC). Mutations in the β-myosin heavy chain (MHC) remain among the most common causes of FHC, with the widely studied R403Q mutation resulting in an especially severe clinical prognosis. In vitro functional studies of cardiac myosin containing the R403Q mutation have revealed significant changes in enzymatic and...
Authors: Niels Volkmann, HongJun Lui, Larnele Hazelwood, Kathleen M. Trybus, Susan Lowey, Dorit Hanein

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