PMC:2728246 / 5312-6214 JSONTXT

{"project":"2_test","denotations":[{"id":"19652920-11414844-56190926","span":{"begin":300,"end":304},"obj":"11414844"},{"id":"19652920-11785752-56190927","span":{"begin":313,"end":317},"obj":"11785752"},{"id":"19652920-19553983-56190928","span":{"begin":319,"end":323},"obj":"19553983"},{"id":"19652920-16276548-56190929","span":{"begin":340,"end":344},"obj":"16276548"},{"id":"19652920-16172390-56190931","span":{"begin":371,"end":375},"obj":"16172390"},{"id":"19652920-19049453-56190932","span":{"begin":388,"end":392},"obj":"19049453"},{"id":"19652920-19415702-56190933","span":{"begin":408,"end":412},"obj":"19415702"},{"id":"19652920-19343225-56190934","span":{"begin":427,"end":431},"obj":"19343225"},{"id":"19652920-18556554-56190935","span":{"begin":685,"end":689},"obj":"18556554"}],"text":"Indeed, RDCs have been recognized to provide a unique perspective on the internal structural fluctuations of proteins even over time scales slower than the correlation time and have thus emerged as the method of choice for studying protein backbone motions in the supra-τc time window (Meiler et al. 2001; Tolman 2001, 2009; Lakomek et al. 2005, 2008a; Bouvignies et al. 2005; Yao et al. 2008; Salmon et al. 2009; Ho and Agard 2009). The relevance of the dynamics occurring in this range was recently highlighted using RDCs, demonstrating that the conformational space attained by human ubiquitin was sufficient to explain the selection of all its known binding partners (Lange et al. 2008). The model-free description of RDC-based dynamics now benefits from robust analysis methods which assess the self-consistency of the dataset and circumvent the pitfall of structural noise (Lakomek et al. 2008a)."}