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Image Search Results
Journal:
Article Title: Biophysical Characterization Reveals Structural Disorder in the Developmental Transcriptional Regulator LBH
doi: 10.1016/j.bbrc.2009.12.032
Figure Lengend Snippet: In silico analysis of LBH. (A) Sequence alignment of LBH proteins from mouse (NCBI ID: NP_084275.3), rat (NP_001123352.1), human (NP_112177.2), orangutan (NP_001125165.1), bovine (NP_001092622.1), dog (XP_853968.1), chicken (NP_001026209.1), finch (XP_002198437.1), Xenopus laevis (NP_001081507.1), salmon (ACI34372.1) and zebrafish (NP_956814.1) showing a high degree of conservation (58–99%) of disorder-promoting amino acid residues in LBH proteins across vertebrate species. Dark shading represents identity at a given amino acid residue, whereas light shading represents amino acid residue similarity. Conserved protein motifs predicted by the primary amino acid sequence [1] are shown on the top of the alignment. NLS = nuclear localization signal. (B) PONDR® VL-XT analysis. Amino acids with PONDR scores ≥0.5 are classified as being in 'disordered' peptide regions and those with scores <0.5 are classified as being in 'ordered' peptide regions.
Article Snippet: The relative order/disorder of the amino acid composition of LBH was predicted by the
Techniques: In Silico, Sequencing, Residue