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The Rags are unusual GTPases in that they function as obligate heterodimers, which consist of Rag A or B bound to Rag C or D. The Rag GTPases interact with m TORC1 and signal amino acid sufficiency by promoting the translocation of m TORC1 to the lysosomal surface, its site of activation.
Thus, SLC38A9 is an excellent candidate for being an amino acid sensor upstream of m TORC1.
The society's Ph D Award for an excellent Ph D thesis is offered for the purpose of encouraging and rewarding outstanding research in the broad field of Imaging Science conducted by our young members.
Our group has been interested in amino acid similarity in the context of peptides binding to proteins.
Given binding data for several peptide ligands, the challenge is to predict the affinity of any peptide of arbitrary sequence.
SLC38A9 forms a supercomplex with Ragulator, the Rag GTPases and the v-ATPase and is necessary for m TORC1 activation by amino acids, particularly arginine.
Overexpression of the full-length protein or just its Ragulator-binding domain makes m TORC1 signaling insensitive to amino acid starvation but does not affect its dependence on Rag activity.
We are happy to support and to dignify the efforts of our young members by raising awareness for their work and to acknowledge their contribution to the interdisciplinary research field.
Experts in peptide: MHC binding studies are often able to estimate the impact of a single residue substitution based on a heuristic understanding of amino acid similarity in an experimental context.
However, PMBEC differs markedly from existing matrices in cases where residue substitution involves a reversal of electrostatic charge.
To demonstrate its usefulness, we have developed a new peptide: MHC class I binding prediction method, using the matrix as a Bayesian prior.