کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7560682 | 1491445 | 2017 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Utilizing tagged paramagnetic shift reagents to monitor protein dynamics by NMR
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کلمات کلیدی
CPMGHSQCCEST19F NMRParamagnetic shiftsCarr-Purcell-Meiboom-Gill - Carr Purcell-Meiboom-GillChemical exchange saturation transfer - انتقال اشباع تبادل شیمیاییPseudocontact shift - تغییر شبه مخروطیConformational dynamics - دینامیک سازگارPCs - رایانه های شخصیCAM - ساخت به کمک کامپیوترpre - قبل ازPulsed EPR - پالس EPRCalmodulin - کالمودولینDeer - گوزنheteronuclear single quantum coherence - یکپارچگی کوانتومی تک هسته ای
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Calmodulin is a ubiquitous calcium sensor protein, known to serve as a critical interaction hub with a wide range of signaling partners. While the holo form of calmodulin (CaM-4Ca2Â +) has a well-defined ground state structure, it has been shown to undergo exchange, on a millisecond timescale, to a conformation resembling that of the peptide bound state. Tagged paramagnetic relaxation agents have been previously used to identify long-range dipolar interactions through relaxation effects on nuclear spins of interest. In the case of calmodulin, this lead to the determination of the relative orientation of the N- and C-terminal domains and the presence of a weakly populated peptide bound like state. Here, we make use of pseudocontact shifts from a tagged paramagnetic shift reagent which allows us to define minor states both in 13C and 15N NMR spectra and through 13C- and 15N-edited 1H-CPMG relaxation dispersion measurements. This is validated by pulsed EPR (DEER) spectroscopy which reveals an ensemble consisting of a compact peptide-bound like conformer, an intermediate peptide-bound like conformer, and a (dumbbell-like) extended ground state conformer of CaM-4Ca2Â +, where addition of the MLCK peptide increases the population of the peptide-bound conformers. This article is part of a Special Issue entitled: Biophysics in Canada, edited by Lewis Kay, John Baenziger, Albert Berghuis and Peter Tieleman.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1865, Issue 11, Part B, November 2017, Pages 1555-1563
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1865, Issue 11, Part B, November 2017, Pages 1555-1563
نویسندگان
Libin Ye, Ned Van Eps, Xiang Li, Oliver P. Ernst, R. Scott Prosser,