Solution Structure Change on NH...O Hydrogen Bond Formation of Oligopeptides Containing Aspartate Anion.
|
Accession number;02A0304377
|
| Title;Solution Structure Change on NH...O Hydrogen Bond Formation of Oligopeptides Containing Aspartate Anion. |
| Author;
ONODA AKIRA
(Osaka Univ., Grad. Sch.)
KUMAGAI KUMIKO
(Pepuchido Kenkyusho)
NAKAJIMA KIICHIRO
(Pepuchido Kenkyusho)
OKAMURA TAKAAKI
(Osaka Univ., Grad. Sch.)
YAMAMOTO HITOSHI
(Osaka Univ., Grad. Sch.)
UEYAMA NORIKAZU
(Osaka Univ., Grad. Sch.)
|
Journal Title;Abstracts. Symposium on Biofunctional Chemistry
|
Journal Code:L0836A
|
ISSN:
|
|
VOL.16th;NO.;PAGE.42-43(2001)
|
| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Asp oligopeptide, Z-FD(COOH)TGSA-NHCy (1), and its aspartate anion, (NEt4){Z-FD(COO)TGSA-NHCy} (2), were synthesized as models for the active site of pepsin. The 1H NMR chemical shifts of amide NHs of Phe, As,. Thr, Gly, Ser, Ala and cyclohexylamino residues of 2 in 10mM CD3CN solution are observed at 6.18, 7.53, 9.16, 8.66, 8.36, 7.42 and 6.83ppm, respectively. The temperature dependence of the amide NH chemical shifts were -5.8, -2.3, -15.0. -4.0, -3.5, -0.72 and -2.4ppb/K, respectively. The results indicate that the Asp NH, Gly NH, Ser NH, Ala NH are involved in the NH...O hydrogen bonds with Asp O.GAMMA.. The NMR structure based on NOE's also supports that these NH's are in the range of the formation of the NH...O hydrogen bonds. These hydrogen bonds force the model peptide, 2, in the aspartate anion state, to give a rigid turn structure which is similar to the structurc in the active site. Detailed information about the NH...O hydrogen bonds was investigated by Asp oligo peptides, 3,5, in the aspartic acid state and 4.6 in the aspartate anion state. (author abst.) |
|
|
|
Related Articles;
|
|
