Louhivuori Martti, Otten Renee, Lindorff-Larsen Kresten, Annila Arto
Department of Physical Sciences, Gustaf Hällströmin katu 2, University of Helsinki, Finland.
J Am Chem Soc. 2006 Apr 5;128(13):4371-6. doi: 10.1021/ja0576334.
The discovery of dilute liquid crystalline media to align biological macromolecules has opened many new possibilities to study protein and nucleic acid structures by NMR spectroscopy. We inspect the basic alignment phenomenon for an ensemble of protein conformations to deduce relative contributions of each member to the residual dipolar coupling signals. We find that molecular fluctuations can affect the alignment and discover a resulting emphasis of certain conformations. However, the internal fluctuations are largely uncorrelated with those of the alignment, implying that proteins have liquidlike molecular surfaces. Furthermore, we consider the implications of a dynamic bias to structure determination using data from the weak alignment method.
稀液晶介质用于排列生物大分子的发现，为通过核磁共振光谱研究蛋白质和核酸结构开辟了许多新的可能性。我们研究了蛋白质构象集合的基本排列现象，以推断每个成员对剩余偶极耦合信号的相对贡献。我们发现分子波动会影响排列，并发现某些构象会因此得到强化。然而，内部波动在很大程度上与排列波动不相关，这意味着蛋白质具有类似液体的分子表面。此外，我们利用弱排列方法的数据，考虑了动态偏差对结构测定的影响。
