Premium
13 C‐NMR chemical shift tensor and hydrogen‐bonded structure of glycine‐containing peptides in a single crystal
Author(s) -
Takeda Naoto,
Kuroki Shigeki,
Kurosu Hiromichi,
Ando Isao
Publication year - 1999
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199907)50:1<61::aid-bip6>3.0.co;2-9
Subject(s) - chemistry , crystallography , hydrogen bond , amide , carbon 13 nmr , hydrogen , magic angle spinning , nuclear magnetic resonance spectroscopy , molecule , stereochemistry , organic chemistry
13 C‐nmr chemical shift tensor components are reported for a 13 C‐labeled Gly 1 amide carbonyl carbon of a glycylglycine (Gly 1 Gly 2 ) single crystal, a GlyGly · HNO 3 single crystal and a GlyGly · HCl · H 2 O single crystal, for which the three‐dimensional crystal structures have already been determined by x‐ray diffraction. The tensor components were measured by changing the angle between the crystal plane and the applied magnetic field by using a goniometer designed in this work for use in conventional 13 C cross‐polarization/magic angle spinning nmr probe. From these experimental data, the principal values of the 13 C chemical shift tensor and its directions for the Gly 1 amide carbonyl carbon were determined. It was found that the 13 C chemical shift tensor components (δ 11 , δ 22 , and δ 33 ) for the Gly 1 amide carbonyl carbon in GlyGly and GlyGly · HNO 3 with a >NH · · · OC< type of hydrogen bond depend on the hydrogen‐bond length and the directions of the δ 22 components of these peptides are along the hydrogen‐bonded >CO bond axis. In addition, the magnitude of the deviation from the bond axis depends on the hydrogen‐bond angle. Further, the experimental result for GlyGly · HCl · H 2 O with a OH · · ·OC< type of hydrogen bond was discussed. © 1999 John Wiley & Sons, Inc. Biopoly 50: 61–69, 1999