caa a22 4500 445325836 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110801xx s 000 0 eng 10.1007/s10858-011-9519-z doi (NATIONALLICENCE)springer-10.1007/s10858-011-9519-z Vögeli Beat Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093, Zürich, Switzerland aut How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar Cα-C′/HN-N cross-correlated relaxation [Elektronische Daten] [Beat Vögeli] Highly precise and accurate measurements of very small NMR cross-correlated relaxation rates, namely those between protein HiN-Ni and Ci−1α-Ci−1′ dipoles, are demonstrated with an error of 0.03s−1 for GB3. Because the projection angles between the two dipole vectors are very close to the magic angle the rates range only from −0.2 to +0.2s−1. Small changes of the average vector orientations have a dramatic impact on the relative values. The rates suggest deviation from idealized peptide plane geometry caused by twists around the C′-N bonds and/or pyramidalization of the nitrogen atoms. A clear alternating pattern along the sequence is observed in β strands 1, 3 and 4 of GB3, where the side chains of almost all residues with large positive rates are solvent exposed. In the α helix all rates are relatively large and positive. Some of the currently most accurate structures of GB3 determined by both high resolution X-ray crystallography and NMR are in satisfactory agreement with the experimental rates in the helix and β strand 3, but not in the loops and the two central strands of the sheet for which no alternating pattern is predicted. Springer Science+Business Media B.V., 2011 Cross-correlated relaxation nationallicence GB3 nationallicence Peptide plane nationallicence ω angle nationallicence Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 315-329 0925-2738 50:4<315 2011 50 10858 https://doi.org/10.1007/s10858-011-9519-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9519-z text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Vögeli Beat Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093, Zürich, Switzerland aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/4(2011-08-01), 315-329 0925-2738 50:4<315 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer