Determination and evaluation of secondary structure content derived from calcium-induced conformational changes in wild-type and mutant mnemiopsin 2 by synchrotron-based Fourier-transform infrared spectroscopy-Reference-Cited by-同舟云学术

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Determination and evaluation of secondary structure content derived from calcium-induced conformational changes in wild-type and mutant mnemiopsin 2 by synchrotron-based Fourier-transform infrared spectroscopy

Published:2020-12 Issue:12 Volume:1868 Page:140528
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Astani Elahe K.,Ersali Sara,Lee Yao-Chang,Lin Pei-Ju,Huang Yen-Chieh,Huang Pei-Yu,Jafarian Vahab,Hosseinkhani Saman,Chen Chun-Jung

Funder

National Synchrotron Radiation Research Center

Tarbiat Modares University

Iran National Science Foundation

Ministerio de Ciencia y Tecnología

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference41 articles.

1. Bioluminescence in the ocean: origins of biological, chemical, and ecological diversity;Widder;Science.,2010

2. Ctenophores of the Baltic and adjacent seas – the invader Mnemiopsis is here! Aquat;Hansson;Invasions.,2006

3. Mechanism of photoinactivation and re-activation in the bioluminescence system of the ctenophore Mnemiopsis;Anctil;Biochem. J.,1984

4. Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state;Liu;Proc. Natl. Acad. Sci. U S A.,2006

5. All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin;Deng;Protein Sci.,2005

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