What's in your buffer? Solute altered millisecond motions detected by solution NMR.
作者： Madeline Wong , Gennady Khirich , J. Patrick Loria
DOI: 10.1021/BI400973E
关键词: RNase PH 、 Protein structure 、 Biophysics 、 Triosephosphate isomerase 、 Molecule 、 Chemistry 、 Millisecond 、 Inorganic chemistry 、 RNase P 、 Chemical shift 、 Ribonuclease
摘要: To date, little work has been conducted on the relationship between solute and buffer molecules conformational exchange motion in enzymes. This study uses solution NMR to examine effects of phosphate, sulfate, acetate comparison MES- HEPES-buffered references chemical shift perturbation millisecond, chemical, or motions enzyme ribonuclease A (RNase A), triosephosphate isomerase (TIM) HisF. The results indicate that addition these solutes a small effect (1)H (15)N shifts for RNase TIM but significant For TIM, Carr-Purcell-Meiboom-Gill relaxation dispersion experiments, however, show solute-dependent changes motions. Some residues loss millisecond relative reference sample upon solute, whereas others experience an enhancement. Comparison parameters obtained from fits data indicates either both equilibrium populations conformations. Furthermore, kinetics are altered many cases. demonstrate common can alter observed play more active role than what is routinely believed.
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