Biophysics and Physicobiology Editors' Choice Award

日本生物物理学会では、前年にBiophysics and Physicobiology誌に掲載された論文（依頼論文は原則対象外）の中から、編集委員会による選考を経て、生物物理学に寄与するユニークな論文に対して、「Biophysics and Physicobiology Editors' Choice Award」を授与します。

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Biophysics and Physicobiology Editors' Choice Award選考規定

第13回Biophysics and Physicobiology Editors' Choice Award受賞論文（2026）

“Improvement in positional accuracy of neural-network predicted hydration sites of proteins by incorporating atomic details of water-protein interactions and site searching algorithm”
Kochi Sato, Masayoshi Nakasako
Biophysics and Physicobiology, Vol. 22, e220004 (2025)

【授賞理由】Editor-in-Charge : Ryo Akiyama

BPPB does not have so many studies based on neural networks and AI. There are some applications based on them for protein structures. However, the application for the hydration structures is rare. Of course, hydration is important in discussing the protein structures and their functions. It seems that the development of a convolutional neural network (CNN) will become more important in the prediction of the probability distribution of hydration water molecules over protein surfaces and in protein cavities. I recommend this research as a candidate because it will encourage other groups that are studying artificial intelligence in structure prediction. In addition, if many biomolecular structure prediction and artificial intelligence projects are nominated for the award, it seems sufficient for one of them to win the award.

“Exploring hydrophilic sequence space to search for uncharted foldable proteins by AlphaFold2”
Naoki Tomita, Hiroki Onoda, Leonard M. G. Chavas, George Chikenji
Biophysics and Physicobiology, Vol. 22, e220005 (2025)

【授賞理由】Editor-in-Charge: Munehito Arai

Proteins generally form compact, globular 3D structures through interactions between hydrophobic amino acids. However, recent reports have shown that threonine rich amino acid sequences can form beta-hairpin structures even when hydrophilic amino acids are abundant. In this study, the authors used AlphaFold2 to investigate whether specific structures can be formed using only hydrophilic amino acids. The results of the theoretical studies suggest that threonine-rich sequences can form specific 3D structures, including β-sandwich structures and hollow triangular structures. These results are interesting, and this editor recommends this paper for the Editor's Choice Award.

“A low-cost electric micromanipulator and its application to single-cell electroporation”
Kazuma Shimizu, Norihiko Nishimura, Manato Oku, Chika Okimura, Yoshiaki Iwadate
Biophysics and Physicobiology, Vol. 22, e220010 (2025)

【授賞理由】Editor-in-Charge: Akihiko Ishijima

This paper describes the construction method and applications of a low-cost electric micromanipulator. It can be constructed at approximately one-fourth the cost of commercially available hydraulic devices and features a practical design that requires no regular maintenance. Using this device, the authors have successfully performed operations such as cutting cell sheets, aspirating single cells, and introducing fluorescent dyes into target cells. It enables precise micromanipulation through pulse control and is presented as a tool that significantly contributes to the analysis of individual cell functions within cell populations.These results are interesting, and this editor recommends this paper for the Editor's Choice Award.

“A method for isolating and cryopreserving intact mitochondria with improved integrity and functionality”
Arima Okutani, Jannatul Naima, Asaka Ogihara, Taihei Motoichi, Ikuroh Ohsawa, Yoshihiro Ohta
Biophysics and Physicobiology, Vol. 22, e220012 (2025)

【授賞理由】Editor-in-Charge: Etsuro Ito

Obtaining isolated mitochondria is important in mitochondrial research. However, conventional isolation procedures often resulted in structural damage, making it difficult to obtain intact mitochondria. Ohta's group has produced a new mitochondrial isolation method that significantly reduces damage to both the inner and outer mitochondrial membranes. In addition, they have also submitted a cryopreservation technique that allows stable freeze-thaw cycles while minimizing the loss of mitochondrial activity. We hope that mitochondria prepared using these methods will promote further progress in mitochondrial research.

“HulaChrimson: A Chrimson-like cation channelrhodopsin discovered using freshwater metatranscriptomics from Lake Hula”
Hiroto Takahashi, Shunki Takaramoto, Takashi Nagata, Shai Fainsod, Yoshitaka Kato, Oded Béjà, Keiichi Inoue
Biophysics and Physicobiology, Vol. 22, e220014 (2025)

【授賞理由】Editor-in-Charge: Hironari Kamikubo

In this study, the authors identified a novel cation channelrhodopsin, "HulaChrimson," which is closely related to Chrimson but exhibits a blue-shifted absorption spectrum. They attempted to identify the amino acid residues responsible for this spectral shift. Although they were unable to identify specific residues that directly control the absorption wavelength, their research suggests that the entire hydrogen-bonding network surrounding the chromophore may determine the absorption wavelength. This provides new insights into the absorption wavelength control mechanism in channelrhodopsins. This work is worthy of recommendation for the "Editor's Choice Awards" of BPPB.

“Visualization of peptidoglycan layer isolated from gliding diderm bacteria, Flavobacterium johnsoniae and Myxococcus xanthus, by quick-freeze deep-etch replica electron microscopy”
Yuhei O. Tahara, Tâm Mignot, Makoto Miyata
Biophysics and Physicobiology, Vol. 22, e220019(2025)

【授賞理由】Editor-in-Charge: Keiichi Namba

Using quick-freeze deep-etch replica electron microscopy, the authors successfully visualized species-dependent different sizes of pores in the peptidoglycan layers of three gram-negative bacteria. They found that the pore size is almost twice larger in Flavobacterium johnsoniae than those of Myxococcus xanthu and E. coli and discussed the mechanism by which those bacteria transmit forces across the peptidoglycan layer to the cell surface for motility.

“Finding differentially expressed genes between cell fates predicted by image-based deep learning”
Tomoaki Okaniwa, Kirill Kryukov, Katsuyuki Shiroguchi
Biophysics and Physicobiology, Vol. 22, e220022 (2025)

【授賞理由】Editor-in-Charge: Hiroko Bannai

This paper proposes a novel technique for predicting cell fate from the microscopic images of unlabeled cells. The authors demonstrate that combining image based deep learning, single-cell selection via microscopy, and RNA sequencing enables the discovery of candidate genes associated with early-stage cell fate determination. This research has broad applicability to studying numerous biological phenomena and represents a paper with significant potential impact, warranting its recommendation for the Editor’s Choice Award.

“Molecular properties of a viral heliorhodopsin, V2HeR2”
Ritsu Mizutori, Kota Katayama, Masae Konno, Keiichi Inoue, Oded Béjà, Hideki Kandori
Biophysics and Physicobiology, Vol. 22, e220024 (2025)

【授賞理由】Editor-in-Charge: Yuki Sudo

The authors investigated a phylogenetically and functionally distinctive microbial rhodopsin, viral heliorhodopsin (V2HeR2), using spectroscopic techniques. In particular, they identified structural distortion of the chromophore retinal and weakening of the hydrogen bond between the Schiff base and its counterion in the presumably functional O photointermediate. The experiments were conducted meticulously, and the results obtained are highly intriguing. Therefore, I recommend this paper as a candidate for the Editor's Choice Awards.

“Schiff base deprotonation and structural changes in a mouse UV sensitive cone visual pigment revealed by FTIR spectroscopy at 77 K”
Yosuke Mizuno, Sora Arai, Kota Katayama, Hideki Kandori
Biophysics and Physicobiology, Vol. 22, e220030 (2025)

【授賞理由】Editor-in-Charge: Keiichi Inoue

Mouse UV-sensitive cone visual pigment is a member of the animal rhodopsin family and is essential for UV recognition in animals. However, the molecular mechanism underlying its UV sensitivity has remained unknown. In this study, using high precision FTIR spectroscopy, the authors demonstrated that an unusually protonated counterion residue is responsible for deprotonating the retinal chromophore, thereby enabling UV absorption. This finding provides a new foundation for understanding the color-tuning mechanisms of animal rhodopsins.

2026年6月
Biophysics and Physicobiology編集委員会