Protein disulfide topology determination through the fusion of mass spectrometric analysis and sequence-based prediction using Dempster-Shafer theory.

ABSTRACT:

Background

Disulfide bonds constitute one of the most important cross-linkages in proteins and significantly influence protein structure and function. At the state-of-the-art, various methodological frameworks have been proposed for identification of disulfide bonds. These include among others, mass spectrometry-based methods, sequence-based predictive approaches, as well as techniques like crystallography and NMR. Each of these frameworks has its advantages and disadvantages in terms of pre-requisites for applicability, throughput, and accuracy. Furthermore, the results from different methods may concur or conflict in parts.

Results

In this paper, we propose a novel and theoretically rigorous framework for disulfide bond determination based on information fusion from differ

SUBMITTER: Singh R 

PROVIDER: S-EPMC3549834 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature