| http://purl.uniprot.org/citations/10526406 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10526406 | http://www.w3.org/2000/01/rdf-schema#comment | "Nuclear spin relaxation monitored by heteronuclear NMR provides a useful method to probe the overall and internal molecular motion for biological macromolecules over a variety of time scales. Nitrogen-15 NMR relaxation parameters have been recorded for the N-terminal domain of the rat T-cell antigen CD2 (CD2d1) in a dilution series from 1.20 mM to 40 microM (pH 6.0, 25 degrees C). The data have been analysed within the framework of the model-free formalism of Lipari and Szabo to understand the molecular origin of severely enhanced transverse relaxation rates found for certain residues. These data revealed a strong dependence of the derived molecular correlation time tau c upon the CD2d1 protein concentration. Moreover, a number of amide NH resonances exhibited exchange broadening and chemical shifts both strongly dependent on protein concentration. These amide groups cluster on the major beta-sheet surface of CD2d1 that coincides with a major lattice contact in the X-ray structure of the intact ectodomain of rat CD2. The complete set of relaxation data fit well to an equilibrium monomer-dimer exchange model, yielding estimates of exchange rate constants (kON = 5000 M-1 s-1; kOFF = 7 s-1) and a dissociation constant (KD approximately 3-6 mM) that is consistent with the difficulty in detecting the weak interactions for this molecule by alternative biophysical methods. The self-association of CD2d1 is essentially invariant to changes in buffer composition and ionic strength and the associated relaxation phenomena cannot be explained as a result of neglecting anisotropic rotational diffusion in the analysis. These observations highlight the necessity to consider low affinity protein self-association interactions as a source of residue specific exchange phenomena in NMR spectra of macromolecular biomolecules, before the assignment of more elaborate intramolecular conformational mechanisms."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.org/dc/terms/identifier | "doi:10.1023/a:1008319917267"xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/author | "Chen H.A."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/author | "Pfuhl M."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/author | "Driscoll P.C."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/author | "Kristensen S.M."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/name | "J Biomol NMR"xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/pages | "307-320"xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/title | "NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1."xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/10526406 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10526406 |
| http://purl.uniprot.org/citations/10526406 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10526406 |
| http://purl.uniprot.org/uniprot/P08921#attribution-6880DEA795E130EA931AC7E209ABC443 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10526406 |
| http://purl.uniprot.org/uniprot/#_P08921-mappedCitation-10526406 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10526406 |
| http://purl.uniprot.org/uniprot/P08921 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10526406 |