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RaptorX. remote homology detection, protein 3D modeling, binding site prediction. Automated webserver and Downloadable program. Biskit. wraps external programs into automated workflow. BLAST search, T-Coffee alignment, and MODELLER construction. ESyPred3D. Template detection, alignment, 3D modeling. Automated webserver.
Many of the same people who created Rosetta@home worked on Foldit. The public beta version was released in May 2008 [10] and has 240,000 registered players. [11]Since 2008, Foldit has participated in Critical Assessment of Techniques for Protein Structure Prediction experiments, submitting its best solutions to targets based on unknown protein structures.
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
A mass spectrometer used for high throughput protein analysis. Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins.Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses.
Proprietary. AnalyzerPro is a vendor-independent software application from SpectralWorks for processing mass spectrometry data. It can process both GC-MS and LC-MS data using qualitative and quantitative data processing and is used in metabolomics with MatrixAnalyzer for the comparison of multiple data sets.
This list of protein subcellular localisation prediction tools includes software, databases, and web services that are used for protein subcellular localization prediction. Some tools are included that are commonly used to infer location through predicted structural properties, such as signal peptide or transmembrane helices , and these tools ...
A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]
A target structure (ribbons) and 354 template-based predictions superimposed (gray Calpha backbones); from CASP8. Critical Assessment of Structure Prediction (CASP), sometimes called Critical Assessment of Protein Structure Prediction, is a community-wide, worldwide experiment for protein structure prediction taking place every two years since 1994.