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  2. Ovalbumin - Wikipedia

    en.wikipedia.org/wiki/Ovalbumin

    Ovalbumin (abbreviated OVA [1]) is the main protein found in egg white, making up approximately 55% of the total protein. [2] Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor. [ 3 ]

  3. List of protein subcellular localization prediction tools

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

    BAR 3.0 is a server for the annotation of protein sequences relying on a comparative large-scale analysis on the entire UniProt. With BAR 3.0 and a sequence you can annotate when possible: function (Gene Ontology), structure (Protein Data Bank), protein domains (Pfam).

  4. List of disorder prediction software - Wikipedia

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

    Computational methods exploit the sequence signatures of disorder to predict whether a protein is disordered, given its amino acid sequence.The table below, which was originally adapted from [1] and has been recently updated, shows the main features of software for disorder prediction.

  5. Protein aggregation predictors - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation_predictors

    sequence - Overall generic and amyloidogenic regions based on the consensus PASTA 2.0 [30] 2014 Web Server - PASTA 2.0: Secondary structure-related. Predicts the most aggregation-prone portions and the corresponding β-strand inter-molecular pairing for multiple input sequences. sequence top pairings and energies, mutations and protein-protein

  6. Molecular-weight size marker - Wikipedia

    en.wikipedia.org/wiki/Molecular-weight_size_marker

    The development of a kit including a molecular-weight size marker based on protein fragments began in 1993. This protein marker, composed of 49 different amino acid sequences, included multidomain proteins, and allowed for the analysis of proteins cleaved at different sites. [9]

  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. De novo peptide sequencing - Wikipedia

    en.wikipedia.org/wiki/De_novo_peptide_sequencing

    Mass of b 2-ions are listed in Table 2, as well as single amino acids that have equal mass to b 2-ions. [15] The mass of b 2-ion = mass of two amino acid residues + 1. Table 2. Mass of b2-ions in peptide fragmentation [16] Identify a sequence ion series by the same mass difference, which matches one of the amino acid residue masses (see Table 1).

  9. Position weight matrix - Wikipedia

    en.wikipedia.org/wiki/Position_weight_matrix

    A PWM has one row for each symbol of the alphabet (4 rows for nucleotides in DNA sequences or 20 rows for amino acids in protein sequences) and one column for each position in the pattern. In the first step in constructing a PWM, a basic position frequency matrix (PFM) is created by counting the occurrences of each nucleotide at each position.