scholarly journals High-pressure 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins

2003 ◽  
Vol 12 (2) ◽  
pp. 207-217 ◽  
Author(s):  
R. Kitahara
2008 ◽  
Vol 9 (4) ◽  
pp. 693-703 ◽  
Author(s):  
Hans Robert Kalbitzer ◽  
Adrian Görler ◽  
Hua Li ◽  
Peter V. Dubovskii ◽  
Wolfgang Hengstenberg ◽  
...  

Carbon ◽  
1984 ◽  
Vol 22 (4-5) ◽  
pp. 433-436 ◽  
Author(s):  
S. Shimokawa ◽  
E. Yamada ◽  
T. Yokono ◽  
S. Iyama ◽  
Y. Sanada

2010 ◽  
Vol 75 (7) ◽  
pp. E417-E425 ◽  
Author(s):  
Maria E. Gonzalez ◽  
Diane M. Barrett ◽  
Michael J. McCarthy ◽  
Frank J. Vergeldt ◽  
Edo Gerkema ◽  
...  

Carbon ◽  
1986 ◽  
Vol 24 (6) ◽  
pp. 771-772 ◽  
Author(s):  
S. Shimokawa ◽  
E. Yamada ◽  
T. Yokono ◽  
J. Yamada ◽  
Y. Sanada ◽  
...  

2004 ◽  
Vol 114 ◽  
pp. 377-378 ◽  
Author(s):  
Y. Shimizu ◽  
K. Miyagawa ◽  
K. Oda ◽  
K. Kanoda ◽  
M. Maesato ◽  
...  

2019 ◽  
Vol 26 (6) ◽  
pp. 449-457
Author(s):  
Ting Song ◽  
Keke Cao ◽  
Yu dan Fan ◽  
Zhichao Zhang ◽  
Zong W. Guo ◽  
...  

Background: The significance of multi-site phosphorylation of BCL-2 protein in the flexible loop domain remains controversial, in part due to the lack of structural biology studies of phosphorylated BCL-2. Objective: The purpose of the study is to explore the phosphorylation induced structural changes of BCL-2 protein. Methods: We constructed a phosphomietic mutant BCL-2(62-206) (t69e, s70e and s87e) (EEEBCL- 2-EK (62-206)), in which the BH4 domain and the part of loop region was truncated (residues 2-61) to enable a backbone resonance assignment. The phosphorylation-induced structural change was visualized by overlapping a well dispersed 15N-1H heteronuclear single quantum coherence (HSQC) NMR spectroscopy between EEE-BCL-2-EK (62-206) and BCL-2. Results: The EEE-BCL-2-EK (62-206) protein reproduced the biochemical and cellular activity of the native phosphorylated BCL-2 (pBCL-2), which was distinct from non-phosphorylated BCL-2 (npBCL-2) protein. Some residues in BH3 binding groove occurred chemical shift in the EEEBCL- 2-EK (62-206) spectrum, indicating that the phosphorylation in the loop region induces a structural change of active site. Conclusion: The phosphorylation of BCL-2 induced structural change in BH3 binding groove.


1991 ◽  
Vol 56 (7) ◽  
pp. 1505-1511 ◽  
Author(s):  
Antonín Lyčka ◽  
Karel Palát
Keyword(s):  
1H Nmr ◽  
H Nmr ◽  

The 15N, 13C, and 1H NMR spectra of the reaction products from arylguanidines with two mols of chloroformate esters have been measured. With application of the corresponding 15N isotopomer it has been proved that the reaction products have the structures IIIa-IIIc.


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