Conclusions and Future Work on the Generalized Type-2 Fuzzy Sugeno Integral

2019 ◽  
pp. 53-55
Author(s):  
Patricia Melin ◽  
Gabriela E. Martinez
Keyword(s):  
Sugeno Integral ◽  
Future Work ◽  
Generalized Type

Generalized Type-2 Fuzzy Logic

2017 ◽  
pp. 3-9
Author(s):  
Claudia I. Gonzalez ◽  
Patricia Melin ◽  
Juan R. Castro ◽  
Oscar Castillo
Keyword(s):  
Fuzzy Logic ◽  
Generalized Type

scholarly journals Exploring the binding properties and structural stability of an opsin in the chytrid Spizellomyces punctatus using comparative and molecular modeling

2017 ◽  
Author(s):  
Steven R Ahrendt ◽  
Edgar Mauricio Medina ◽  
Chia-en A Chang ◽  
Jason E Stajich
Keyword(s):  
Molecular Modeling ◽  
Structural Characteristics ◽  
Sequence Similarity ◽  
Ligand Docking ◽  
Binding Properties ◽  
Function Relationship ◽  
Relationship Of ◽  
Future Work

Background. Opsin proteins are seven transmembrane receptor proteins which detect light. Opsins can be classified into two types and share little sequence identity: type 1, typically found in bacteria, and type 2, primarily characterized in metazoa. The type 2 opsins (Rhodopsins) are a subfamily of G-protein coupled receptors (GPCRs), a large and diverse class of seven transmembrane proteins and are generally restricted to metazoan lineages. Fungi use light receptors including opsins to sense the environment and transduce signals for developmental or metabolic changes. Opsins characterized in the Dikarya (Ascomycetes and Basidiomycetes) are of the type 1 bacteriorhodopsin family but the early diverging fungal lineages have not been as well surveyed. We identified by sequence similarity a rhodopsin-like GPCR in genomes of early diverging chytrids and examined the structural characteristics of this protein to assess its likelihood to be homologous to animal rhodopsins and bind similar chromophores. Methods. We used template-based structure modeling, automated ligand docking, and molecular modeling to assess the structural and binding properties of an identified opsin-like protein found in Spizellomyces punctatus, a unicellular, flagellated species belonging to Chytridiomycota, one of the earliest diverging fungal lineages. We tested if sequence and inferred structure were consistent with a solved crystal structure of a type 2 rhodopsin from the squid Todarodes pacificus. Results. Our results indicate that the Spizellomyces opsin has structural characteristics consistent with functional animal type 2 rhodopsins and is capable of maintaining a stable structure when associated with the retinaldehyde chromophore, specifically the 9-cis­-retinal isomer. Together, these results support further the homology of Spizellomyces opsins to animal type 2 rhodopsins. Discussion. This represents the first test of structure/function relationship of a type 2 rhodopsin identified in early branching fungal lineages, and provides a foundation for future work exploring pathways and components of photoreception in early fungi.

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