caa a22 4500 477136303 CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970101xx s 000 0 eng 10.1023/A:1018627702855 doi (NATIONALLICENCE)springer-10.1023/A:1018627702855 LeMaster David Department of Biochemistry and National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, 420 Henry Mall, 53706, Madison, WI, U.S.A aut Assessment of protein solution versus crystal structure determination using spin- diffusion-suppressed NOE and heteronuclear relaxation data [Elektronische Daten] [David LeMaster] A spin-diffusion-suppressed NOE buildup series has been measured for E. coli thioredoxin.The extensive 13C and 15N relaxation data previously reported for this protein allow fordirect interpretation of dynamical contributions to the 1H-1H cross-relaxation rates for a largeproportion of the NOE cross peaks. Estimates of the average accuracy for these derived NOEdistances are bounded by 4% and 10%, based on a comparison to the corresponding X-raydistances. An independent fluctuation model is proposed for prediction of the dynamicalcorrections to 1H-1H cross-relaxation rates, based solely on experimental structural andheteronuclear relaxation data. This analysis is aided by the demonstration that heteronuclearorder parameters greater than 0.6 depend only on the variance of the H-X bond orientation,independent of the motional model in either one- or two-dimensional diffusion (i.e., 1− S2 = 3/4 sin2 2 θσ). The combination of spin-diffusion-suppressed NOEdata and analysis of dynamical corrections to 1H-1H cross-relaxation rates based onheteronuclear relaxation data has allowed for a detailed interpretation of various discrepanciesbetween the reported solution and crystal structures. Kluwer Academic Publishers, 1997 Protein deuteration nationallicence Spin diffusion nationallicence Heteronuclear relaxation nationallicence Structural analysis nationallicence Journal of Biomolecular NMR Kluwer Academic Publishers 9/1(1997-01-01), 79-93 0925-2738 9:1<79 1997 9 10858 https://doi.org/10.1023/A:1018627702855 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018627702855 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- LeMaster David Department of Biochemistry and National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, 420 Henry Mall, 53706, Madison, WI, U.S.A aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/1(1997-01-01), 79-93 0925-2738 9:1<79 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer