NifFinder:使SWeePNif

Bruno Thiago de Lima Nichio1,2, Roxana Beatriz Ribeiro Chaves2, Jeroniza Nunes Marchaukoski1

  • 1Laboratory of Artificial Intelligence Applied to Bioinformatics (AIBIA), Professional and Technical Education Sector (SEPT) - UFPR, Curitiba, Paraná, 81520-260, Brazil.

Bioinformatics advances
|December 1, 2025
PubMed
概括

NifFinder使用SWeeP矢量和神经网络准确识别多达24种固定 (Nif) 蛋白. 该工具增强了全基因组Nif蛋白发现,用于农业可持续性和进化研究.

相关概念视频

Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
14.0K
Improving Translational Accuracy02:07

Improving Translational Accuracy

3.5K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.0K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.0K