1 H , 13 C and 15 N backbone and side - chain resonance assignments of Drosophila melanogaster Ssu 72

Title Backbone and side - chain 1 H , 15 N and 13 C resonance assignments of S 18 Y mutant of ubiquitin carboxy

Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3

Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.

Automated protein fold determination using a minimal NMR constraint strategy.

Determination of precise and accurate protein structures by NMR generally requires weeks or even months to acquire and interpret all the necessary NMR data. However, even medium-accuracy fold information can often provide key clues about protein evolution and biochemical function(s). In this article we describe a largely automatic strategy for rapid determination of medium-accuracy protein back...

Title Backbone and side - chain 1 H , 15 N and 13 C resonance assignments of S 18 Y mutant of ubiquitin carboxy - terminal hydrolase

(1)H, (13)C, and (15)N NMR assignments for the Bacillus subtilis yndB START domain.

The steroidogenic acute regulatory-related lipid transfer (START) domain is found in both eukaryotes and prokaryotes, with putative functions including signal transduction, transcriptional regulation, GTPase activation and thioester hydrolysis. Here we report the near complete (1)H, (15)N and (13)C backbone and side chain NMR resonance assignments for the Bacillus subtilis START domain protein ...