998 resultados para pseudoscalar Cornell potential


Relevância:

30.00% 30.00%

Publicador:

Resumo:

Available on demand as hard copy or computer file from Cornell University Library.

Relevância:

30.00% 30.00%

Publicador:

Resumo:

Following up on earlier work on the $q\bar{q}$-bound-state problem using a covariant, chiral-symmetric formalism based upon the Covariant Spectator Theory, we study the heavy–light case for both pseudoscalar and vector mesons. Derived directly in Minkowski space, our approach approximates the full Bethe–Salpeter-equation, taking into account, effectively, the contributions of both ladder and crossed ladder diagrams in the kernel. Results for several mass spectra using a relativistic covariant generalization of a Cornell plus a constant potential to model the interquark interaction are given and discussed.

Relevância:

20.00% 20.00%

Publicador:

Resumo:

The tissue kallikreins are serine proteases encoded by highly conserved multigene families. The rodent kallikrein (KLK) families are particularly large, consisting of 13 26 genes clustered in one chromosomal locus. It has been recently recognised that the human KLK gene family is of a similar size (15 genes) with the identification of another 12 related genes (KLK4-KLK15) within and adjacent to the original human KLK locus (KLK1-3) on chromosome 19q13.4. The structural organisation and size of these new genes is similar to that of other KLK genes except for additional exons encoding 5 or 3 untranslated regions. Moreover, many of these genes have multiple mRNA transcripts, a trait not observed with rodent genes. Unlike all other kallikreins, the KLK4-KLK15 encoded proteases are less related (25–44%) and do not contain a conventional kallikrein loop. Clusters of genes exhibit high prostatic (KLK2-4, KLK15) or pancreatic (KLK6-13) expression, suggesting evolutionary conservation of elements conferring tissue specificity. These genes are also expressed, to varying degrees, in a wider range of tissues suggesting a functional involvement of these newer human kallikrein proteases in a diverse range of physiological processes.