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  2. List of protein subcellular localization prediction tools

    en.wikipedia.org/wiki/List_of_protein_sub...

    The University of Minnesota Pathway Prediction System (UM-PPS) is a web tool that recognizes functional groups in organic compounds that are potential targets of microbial catabolic reactions and predicts transformations of these groups based on biotransformation rules. Multi-level predictions are made. (bio.tools entry) [116]

  3. Palmitoylation - Wikipedia

    en.wikipedia.org/wiki/Palmitoylation

    Palmitoylation of Gephyrin Controls Receptor Clustering and Plasticity of GABAergic Synapses [1] In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane ...

  4. Protein aggregation predictors - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation_predictors

    Prediction of B-strand propensity score to locate in the amyloid fibril. sequence - beta-strand formation Hexapeptide Conformational Energy /Pre-amyl [7] 2007 Web Server- AMYLPRED2: Secondary structure-related

  5. List of protein secondary structure prediction programs

    en.wikipedia.org/wiki/List_of_protein_secondary...

    Name Method description Type Link Initial release RaptorX-SS8 : predict both 3-state and 8-state secondary structure using conditional neural fields from PSI-BLAST profiles ...

  6. List of disorder prediction software - Wikipedia

    en.wikipedia.org/wiki/List_of_disorder...

    Based on five amino acids, the folding variations along sequence are presented by Protein Folding Shape Code (PFSC) in Protein Folding Variation Matrix (PFVM). No Yes, Login=public; Password=public; select “Prediction” SPOT-Disorder2 [3] 2020 Per-residue probability of a sequence residue being disordered.

  7. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    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).

  8. Protein function prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_function_prediction

    The importance and prevalence of computational prediction of gene function is underlined by an analysis of 'evidence codes' used by the GO database: as of 2010, 98% of annotations were listed under the code IEA (inferred from electronic annotation) while only 0.6% were based on experimental evidence.

  9. Precision livestock farming - Wikipedia

    en.wikipedia.org/wiki/Precision_livestock_farming

    The development of quantitative methods for livestock production includes mathematical modelling based in plant-herbivore or predator-prey models to forecast and optimise meat production. An example is the Predator-Prey Grassland Livestock Model (PPGL) [ 7 ] to address the dynamics of the combined grass-animals system as a predator-prey ...

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