著者
太田 啓介
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.58, no.5, pp.265-269, 2018 (Released:2018-09-29)
参考文献数
4
被引用文献数
1 1
著者
加藤 英明 濡木 理
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.53, no.5, pp.246-249, 2013 (Released:2013-09-25)
参考文献数
20
被引用文献数
1

Channelrhodopsin (ChR) is a light-gated cation channel derived from algae. Since the inward flow of cations triggers the neuron firing, neurons expressing ChRs can be optically controlled even within freely moving mammals. Although ChR has been broadly applied to neuroscience research, little is known about its molecular mechanisms. We determined the crystal structure of chimeric ChR at 2.3 Å resolution and revealed its molecular architecture. The integration of structural and electrophysiological analyses provided insight into the molecular basis for the channel function of ChR, and paved the way for the principled design of ChR variants with novel properties.
著者
菊川 峰志
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.61, no.1, pp.012-015, 2021 (Released:2021-01-29)
参考文献数
12

Cl–-pump rhodopsin is the second discovered microbial rhodopsin and functions as light-driven Cl– pump. The physiological significance of the Cl– pump has not been fully resolved. However, its functional mechanism has been studied as a model system of anion transporters. In this review, the variation and functional mechanisms of Cl–-pump rhodopsins were summarized. After 2014, novel Cl–-pump groups were discovered in marine and terrestrial bacteria and were revealed to have unique characteristics. The most recently identified protein has close similarity with the H+-pump rhodopsin and begins to pump H+ outwardly by only a single amino acid replacement.
著者
久保田 浩行 黒田 真也
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.53, no.4, pp.184-189, 2013 (Released:2013-07-25)
参考文献数
18

Cellular responses, such as cell fate decision and hormonal regulations, can be regulated by distinct temporal patterns of signaling molecules. However, how temporal patterns of signaling molecules determine the cellular responses remains largely unknown. Recently, we have proposed the concept of “temporal coding”, by which a single molecular species can encode multiple information through its temporal patterns. We found that signaling pathways can process information of stimulation patterns depending on their network motif and kinetics, and cells can regulate downstream molecules depending on stimulation pattern. Thus, “temporal coding” appears to serve as an information-embedding strategy to elicit specific cellular responses.
著者
古賀 理恵 古賀 信康
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.60, no.6, pp.325-330, 2020 (Released:2020-11-28)
参考文献数
26

Protein design holds promise for applications such as control of cells, therapeutics, new enzymes and protein-based materials. Recently, rational design of protein molecules has made a great progress, guided by the consistency principle proposed by Nobuhiro Gō in 1983: local and non-local interactions consistently favor the same folded conformation. We discovered a set of rules for designing ideal protein structures stabilized by consistent local and non-local interactions. The rules enabled the de novo design of amino acid sequences having the funnel-shaped energy landscapes toward the desired target structures. Various ideal protein structures have been created using the rules.
著者
織田 昌幸
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.60, no.6, pp.342-345, 2020 (Released:2020-11-28)
参考文献数
14

A cutinase-like enzyme from a thermophilic isolate, Saccharomonospora viridis AHK190, Cut190, has the ability to depolymerize polyethylene terephthalate (PET). The catalytic activity and thermal stability of Cut190 are increased by Ca2+ binding. The structural analysis of Cut190 mutants in complex with metal ions and substrates elucidated the reaction mechanism regulated by Ca2+. The metal ion-binding properties, analyzed using isothermal titration calorimetry were correlated with the effects on Cut190 activity and stability, which could be improved using protein engineering. The Cut190 mutant will be used for PET chemical recycling.