[1] GRONENBORN A M, FILPULA D R, ESSIG N Z, et al. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G[J]. Science, 1991, 253(5020):657-661.[2] NADAUD P S, HELMUS J J, HOFER N, et al. Long-range structural restraints in spin-labeled proteins probed by solid-state nuclear magnetic resonance spectroscopy[J]. J Am Chem Soc, 2007, 129(24):7502-7503.[3] NADAUD P S, HELMUS J J, KALL S L, et al. Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins[J]. J Am Chem Soc, 2009, 131(23):8108-8120.[4] NADAUD P S, SENGUPTA I, HELMUS J J, et al. Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of <sup>15</sup>N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR[J]. J Biomol NMR, 2011, 51(3):293-302.[5] SENGUPTA I, NADAUD P S, HELMUS J J, et al. Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy[J]. Nat Chem, 2012, 4(5):410-417.[6] SENGUPTA I, NADAUD P S, JARONIEC C P. Protein structure determination with paramagnetic solid-state NMR spectroscopy[J]. Acc Chem Res, 2013, 46(9):2117-2126.[7] LI J P, PILLA K B, LI Q F, et al. Magic angle spinning NMR structure determination of proteins from pseudocontact shifts[J]. J Am Chem Soc, 2013, 135(22):8294-8303.[8] SENGUPTA I, GAO M, ARACHCHIGE R J, et al. Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(Ⅱ) binding tag[J]. J Biomol NMR, 2015, 61(1):1-6.[9] TAMAKI H, EGAWA A, KIDO K, et al. Structure determination of uniformly <sup>13</sup>C, <sup>15</sup>N labeled protein using qualitative distance restraints from MAS solid-state <sup>13</sup>C-NMR observed paramagnetic relaxation enhancement[J]. J Biomol NMR, 2016, 64(1):87-101.[10] MUNTENER T, HAUSSINGER D, SELENKO P, et al. In-cell protein structures from 2D NMR experiments[J]. J Phys Chem Lett, 2016, 7(14):2821-2825.[11] PAN B B, YANG F, YE Y S, et al. 3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy[J]. Chem Commun, 2016, 52(67):10237-10240.[12] SEEWALD M J, PICHUMANI K, STOWELL C, et al. The role of backbone conformational heat capacity in protein stability:temperature dependent dynamics of the B1 domain of Streptococcal protein G[J]. Protein Sci, 2000, 9(6):1177-1193.[13] BARCHI JR J J, GRASBERGER B, GRONENBORN A M, et al. Investigation of the backbone dynamics of the IgG-binding domain of streptococcal protein G by heteronuclear two-dimensional <sup>1</sup>H-<sup>15</sup>N nuclear magnetic resonance spectroscopy[J]. Protein Sci, 1994, 3(1):15-21.[14] TUNNICLIFFE R B, WABY J L, WILLIAMS R J, et al. An experimental investigation of conformational fluctuations in proteins G and L[J]. Structure, 2005, 13(11):1677-1684.[15] JEE J, BYEON I J, LOUIS J M, et al. The point mutation A34F causes dimerization of GB1[J]. Proteins, 2008, 71(3):1420-1431.[16] MCCALLISTER E L, ALM E, BAKER D. Critical role of beta-hairpin formation in protein G folding[J]. Nat Struct Biol, 2000, 7(8):669-673.[17] KARANICOLAS J, BROOKS C L. The origins of asymmetry in the folding transition states of protein L and protein G[J]. Protein Sci, 2002, 11(10):2351-2361.[18] WILTON D J, TUNNICLIFFE R B, KAMATARI Y O, et al. Pressure-induced changes in the solution structure of the GB1 domain of protein G[J]. Proteins, 2008, 71(3):1432-1440.[19] GRONENBORN A M, FILPULA D R, ESSIG N Z, et al. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein-G[J]. Science, 1991, 253(5020):657-661.[20] THORDARSON P. Determining association constants from titration experiments in supramolecular chemistry[J]. Chem Soc Rev, 2011, 40(3):1305-1323.[21] GRZESIEK S, BAX A, CLORE G M, et al. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase[J]. Nat Struct Biol, 1996, 3(4):340-345.[22] CHEEVER M L, SATO T K, DE BEER T, et al. Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes[J]. Nat Cell Biol, 2001, 3(7):613-618.[23] FISHER R D, WANG B, ALAM S L, et al. Structure and ubiquitin binding of the ubiquitin-interacting motif[J]. J Biol Chem, 2003, 278(31):28976-82894.[24] OTTING G. Protein NMR using paramagnetic ions[J]. Annu Rev Biophys, 2010, 39:387-405.[25] KUSZEWSKI J, GRONENBORN A M, CLORE G M. Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration[J]. J Am Chem Soc, 1999, 121(10):2337-2338.[26] SCHMITZ C, STANTON-COOK M J, SU X C, et al. Numbat:an interactive software tool for fitting Delta chi-tensors to molecular coordinates using pseudocontact shifts[J]. J Biomol NMR, 2008, 41(3):179-189.[27] WILLIAMS R J P. Chemical selection of elements by cells[J]. Coordin Chem Rev, 2001, 216, 217:583-595. |