Sciweavers

526 search results - page 5 / 106
» High-throughput modeling and analysis of protein structural ...
Sort
View
BMCBI
2010
118views more  BMCBI 2010»
13 years 8 months ago
Computing H/D-Exchange rates of single residues from data of proteolytic fragments
Background: Protein conformation and protein/protein interaction can be elucidated by solution-phase Hydrogen/ Deuterium exchange (sHDX) coupled to high-resolution mass analysis o...
Ernst Althaus, Stefan Canzar, Carsten Ehrler, Mark...
BMCBI
2005
126views more  BMCBI 2005»
13 years 7 months ago
HomoMINT: an inferred human network based on orthology mapping of protein interactions discovered in model organisms
Background: The application of high throughput approaches to the identification of protein interactions has offered for the first time a glimpse of the global interactome of some ...
Maria Persico, Arnaud Ceol, Caius Gavrila, Robert ...
BMCBI
2010
160views more  BMCBI 2010»
13 years 8 months ago
Identification of functional hubs and modules by converting interactome networks into hierarchical ordering of proteins
Background: Protein-protein interactions play a key role in biological processes of proteins within a cell. Recent high-throughput techniques have generated protein-protein intera...
Young-Rae Cho, Aidong Zhang
JCC
2008
92views more  JCC 2008»
13 years 7 months ago
Fast procedure for reconstruction of full-atom protein models from reduced representations
: We introduce PULCHRA, a fast and robust method for the reconstruction of full-atom protein models starting from a reduced protein representation. The algorithm is particularly su...
Piotr Rotkiewicz, Jeffrey Skolnick
DASFAA
2005
IEEE
209views Database» more  DASFAA 2005»
14 years 1 months ago
PADS: Protein Structure Alignment Using Directional Shape Signatures
A novel approach for similarity search on the protein structure databases is proposed. PADS (Protein Alignment by Directional shape Signatures) incorporates the three dimensional ...
S. Alireza Aghili, Divyakant Agrawal, Amr El Abbad...