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This classification is then taken into account for the different data views and all supported automatic analysis functions. RNASeqExpressionBrowser is a web-based tool which provides means for the search and visualization of RNA-seq expression data (e.g. based on sequence-information or domain annotations).
Conserved signature inserts and deletions (CSIs) in protein sequences provide an important category of molecular markers for understanding phylogenetic relationships. [1] [2] CSIs, brought about by rare genetic changes, provide useful phylogenetic markers that are generally of defined size and they are flanked on both sides by conserved regions to ensure their reliability.
A logarithmic chart allows only positive values to be plotted. A square root scale chart cannot show negative values. x: the x-values as a comma-separated list, for dates and time see remark in xType and yType; y or y1, y2, …: the y-values for one or several data series, respectively. For pie charts y2 denotes the radius of the corresponding ...
Ab Initio gene prediction is an intrinsic method based on gene content and signal detection. Because of the inherent expense and difficulty in obtaining extrinsic evidence for many genes, it is also necessary to resort to ab initio gene finding, in which the genomic DNA sequence alone is systematically searched for certain tell-tale signs of protein-coding genes.
A conserved non-coding sequence (CNS) is a DNA sequence of noncoding DNA that is evolutionarily conserved. These sequences are of interest for their potential to regulate gene production. [1] CNSs in plants [2] and animals [1] are highly associated with transcription factor binding sites and other cis-acting regulatory elements.
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There are two common methods in which to construct a DNA molecular-weight size marker. [3] One such method employs the technique of partial ligation. [3] DNA ligation is the process by which linear DNA pieces are connected to each other via covalent bonds; more specifically, these bonds are phosphodiester bonds. [4]
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).