scholarly journals Solution NMR Study on Functional Mechanism of Membrane Proteins

2013 ◽  
Vol 53 (5) ◽  
pp. 236-241
Author(s):  
Masanori OSAWA ◽  
Shunsuke IMAI ◽  
Koh TAKEUCHI ◽  
Ichio SHIMADA
Keyword(s):  
Membrane Proteins ◽  
Solution Nmr ◽  
Functional Mechanism ◽  
Nmr Study

Expression and Solution NMR Study of Multi-site Phosphomimetic Mutant BCL-2 Protein

2019 ◽  
Vol 26 (6) ◽  
pp. 449-457
Author(s):  
Ting Song ◽  
Keke Cao ◽  
Yu dan Fan ◽  
Zhichao Zhang ◽  
Zong W. Guo ◽  
...  
Keyword(s):  
Structural Change ◽  
Structural Biology ◽  
Quantum Coherence ◽  
Structural Changes ◽  
Solution Nmr ◽  
Flexible Loop ◽  
Loop Region ◽  
Loop Domain ◽  
Nmr Study ◽  
Binding Groove

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.

Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments

2019 ◽  
pp. 143-185 ◽  
Author(s):  
Erik Henrich ◽  
Frank Löhr ◽  
Julija Mezhyrova ◽  
Aisha Laguerre ◽  
Frank Bernhard ◽  
...  
Keyword(s):  
Synthetic Biology ◽  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

Solution NMR Study of Liquid Silk

2016 ◽  
Vol 72 (4) ◽  
pp. P-208-P-208
Author(s):  
YU SUZUKI
Keyword(s):  
Solution Nmr ◽  
Nmr Study

Two-dimensional crystallization of membrane proteins

1992 ◽  
Vol 25 (1) ◽  
pp. 1-49 ◽  
Author(s):  
W. Kühlbrandt
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Molecular Mass ◽  
Solution Nmr ◽  
Two Dimensional ◽  
Foreseeable Future ◽  
Nmr Techniques

In spite of several great breakthroughs, the overall rate of progress in determining high-resolution structures of membrane proteins has been slow. This is entirely due to the scarcity of suitable, well-ordered crystals. Most membrane proteins are multimeric complexes with a composite molecular mass in excess of 50000 Da which puts them outside the range of current solution NMR techniques. For the foreseeable future, detailed information about the structure of large membrane proteins will therefore depend on crystallographic methods.

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