PMC:2728246 / 2804-4147 JSONTXT

{"project":"2_test","denotations":[{"id":"19652920-1314645-56190904","span":{"begin":393,"end":397},"obj":"1314645"},{"id":"19652920-16683749-56190905","span":{"begin":416,"end":420},"obj":"16683749"},{"id":"19652920-16075427-56190906","span":{"begin":440,"end":444},"obj":"16075427"},{"id":"19652920-16984199-56190907","span":{"begin":446,"end":450},"obj":"16984199"},{"id":"19652920-17488010-56190908","span":{"begin":463,"end":467},"obj":"17488010"},{"id":"19652920-17034251-56190909","span":{"begin":595,"end":599},"obj":"17034251"},{"id":"19652920-17973392-56190910","span":{"begin":618,"end":622},"obj":"17973392"},{"id":"19652920-19049457-56190911","span":{"begin":837,"end":841},"obj":"19049457"},{"id":"19652920-16984151-56190912","span":{"begin":855,"end":859},"obj":"16984151"},{"id":"19652920-11841314-56190913","span":{"begin":1100,"end":1104},"obj":"11841314"},{"id":"19652920-11457242-56190914","span":{"begin":1124,"end":1128},"obj":"11457242"},{"id":"19652920-12061716-56190915","span":{"begin":1150,"end":1154},"obj":"12061716"},{"id":"19652920-15038751-56190916","span":{"begin":1172,"end":1176},"obj":"15038751"},{"id":"19652920-16267559-56190917","span":{"begin":1197,"end":1201},"obj":"16267559"},{"id":"19652920-16984199-56190918","span":{"begin":1221,"end":1225},"obj":"16984199"},{"id":"19652920-10625431-56190919","span":{"begin":1288,"end":1292},"obj":"10625431"},{"id":"19652920-16893184-56190920","span":{"begin":1311,"end":1315},"obj":"16893184"},{"id":"19652920-19422234-56190921","span":{"begin":1337,"end":1341},"obj":"19422234"}],"text":"Similarly to the residue-specific investigation of mobility in the backbone, side chain disorder has also been studied with residue resolution as a result of development of NMR methodologies targeting methyl groups. Measurement of relaxation rates of 13C and 2H in isotope-labeled methyl groups are now being used routinely to understand side chain dynamics (Lee et al. 1999; Schneider et al. 1992; Igumenova et al. 2006; Tugarinov and Kay 2005, 2006; Xue et al. 2007), while methods for the quantitative interpretation of side chain order parameters are still being improved (Meirovitch et al. 2006; Showalter et al. 2007). Solid-state NMR relaxation techniques have also been used to study methyl group dynamics and suggested a high concordance between the motions for a protein in solution and in the aggregated state (Agarwal et al. 2008; Reif et al. 2006). Recent interests in the hydrophobic mechanism of folding, packing and recognition of protein-ligand, protein-protein and other protein assemblies have used 2H relaxation rates in methyl groups to describe their flexibility (Mulder et al. 2002; Skrynnikov et al. 2001; Mittermaier and Kay 2002; Korzhnev et al. 2004; Eisenmesser et al. 2005; Tugarinov and Kay 2006) and residual conformation entropy of side chains (Lee et al. 2000; Frederick et al. 2006; Li and Brüschweiler 2009)."}