How Does a Microbial Rhodopsin RxR Realize Its Exceptionally High Thermostability with the Proton-Pumping Function Being Retained?

We often encounter a case where two proteins, whose amino-acid sequences are similar, are quite different with regard to the thermostability. As a striking example, we consider the two seven-transmembrane proteins: recently discovered Rubrobacter xylanophilus rhodopsin (RxR) and long-known bacterior...

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Veröffentlicht in:	The journal of physical chemistry. B 2020-02, Vol.124 (6), p.990-1000
Hauptverfasser:	Hayashi, Tomohiko, Yasuda, Satoshi, Suzuki, Kano, Akiyama, Tomoki, Kanehara, Kanae, Kojima, Keiichi, Tanabe, Mikio, Kato, Ryuichi, Senda, Toshiya, Sudo, Yuki, Murata, Takeshi, Kinoshita, Masahiro
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinobacteria - chemistry Crystallography, X-Ray Halobacterium salinarum - chemistry Models, Molecular Protein Folding Proton Pumps - chemistry Rhodopsins, Microbial - chemistry Solvents - chemistry Thermodynamics
Online-Zugang:	Volltext
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