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BCrystal: An Interpretable Sequence-Based Protein Crystallization Predictor.

08:00 EDT 11th October 2019 | BioPortfolio

Summary of "BCrystal: An Interpretable Sequence-Based Protein Crystallization Predictor."

X-ray crystallography has facilitated the majority of protein structures determined to date. Sequence-based predictors that can accurately estimate protein crystallization propensities would be highly beneficial to overcome the high expenditure, large attrition rate, and to reduce the trial-and-error settings required for crystallization.

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This article was published in the following journal.

Name: Bioinformatics (Oxford, England)
ISSN: 1367-4811
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Medical and Biotech [MESH] Definitions

A process that includes the determination of an amino acid sequence of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.

An anatomic severity scale based on the Abbreviated Injury Scale (AIS) and developed specifically to score multiple traumatic injuries. It has been used as a predictor of mortality.

A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.

A conserved AMINO ACID SEQUENCE located in the intracellular domains of a family of transmembrane proteins that negatively regulate the signal transduction processes emanating from transmembrane proteins containing IMMUNORECEPTOR TYROSINE-BASED ACTIVATION MOTIFS. The CONSENSUS SEQUENCE of this motif is I(or V)LXYXXL(or V) (where X denotes any amino acid). Also known as ITIM motifs.

Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.

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