967 resultados para Glycoside hydrolase family 16


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Top row: Alexander Gans and his wife

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N-linked glycosylation has a profound effect on the proper folding, oligomerization and stability of glycoproteins. These glycans impart many properties to proteins that may be important for their proper functioning, besides having a tendency to exert a chaperone-like effect on them. Certain glycosylation sites in a protein however, are more important than other sites for their function and stability. It has been observed that some N-glycosylation sites are conserved over families of glycoproteins over evolution, one such being the tyrosinase related protein family. The role of these conserved N-glycosylation sites in their trafficking, sorting, stability and activity has been examined here. By scrutinizing the different glycosylation sites on this family of glycoproteins it was inferred that different sites in the same family of polypeptides can perform distinct functions and conserved sites across the paralogues may perform diverse functions.

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l-r: Thekla Oppenheimer-Benedick, Jenny Oppenheimer-Frank, Fanny Oppenheimer and Adele Oppenheimer-Nathan

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l-r: Sisters Adele Oppenheimer-Nathan, Thekla Oppenheimer-Benedick, Jenny Oppenheimer-Frank and their mother Fanny Oppenheimer

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Verso: handwritten correspondence

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Digital Image

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Digital Image

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Family tree and genealogy of Jacob family in Stavenhagen, Mecklenburg, 1690-1975.

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Double Wedding Ceremony Heimann-Rosenfelder August 17, 1909