Výsledky vyhledávání - "Raiji Kawade"

Anion solvation enhanced by positive supercharging mutations preserves thermal stability of an antibody in a wide pH range

Autor: Daisuke Kuroda, Kouhei Tsumoto, Keisuke Kasahara, Raiji Kawade, Aki Tanabe, Satoru Nagatoishi

Publikováno v: Biochemical and biophysical research communications. 563

Proteins function through interactions with other molecules. In protein engineering, scientists often engineer proteins by mutating their amino acid sequences on the protein surface to improve various physicochemical properties. “Supercharging” i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aa243fd55e0daa8fccadbafa06dcfcc
https://pubmed.ncbi.nlm.nih.gov/34058475

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Roles of the disulfide bond between the variable and the constant domains of rabbit immunoglobulin kappa chains in thermal stability and affinity

Autor: Toshiaki Maruyama, Raiji Kawade, C.J. Okumura, Hiroki Akiba, Kouhei Tsumoto, Kevin C. Entzminger

Publikováno v: Protein Engineering, Design and Selection. 31:243-247

Rabbit antibodies show unique structural characteristics in that kappa chains have an inter-domain disulfide bond between the variable and constant domains. Here we characterized this disulfide bond from physicochemical viewpoints both in stability a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb8762e5a4ea4da59f3c46fc6124a9d
https://doi.org/10.1093/protein/gzy008

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How the protonation state of a phosphorylated amino acid governs molecular recognition: insights from classical molecular dynamics simulations

Autor: Daisuke Kuroda, Raiji Kawade, Kouhei Tsumoto

Publikováno v: FEBS lettersReferences. 594(5)

Physicochemical properties of proteins are controlled mainly by post-translational modifications such as amino acid phosphorylation. Although molecular dynamics simulations have been shown to be a valuable tool for studying the effects of phosphoryla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0317952afc765a3a73fc4c04daddf69c
https://pubmed.ncbi.nlm.nih.gov/31713840

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A Chemically Inducible Helper Module for Detecting Protein-Protein Interactions with Tunable Sensitivity Based on KIPPIS

Autor: Masahiro Kawahara, Raiji Kawade, Daiki Kashima, Teruyuki Nagamune

Publikováno v: Analytical chemistry. 89(9)

As protein–protein interactions (PPIs) play essential roles in regulating their functional consequences in cells, methods to detect PPIs in living cells are desired for correct understanding of intracellular PPIs and pharmaceutical development ther

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::add24bdcbfeb4371bb5b676db0447de9
https://pubmed.ncbi.nlm.nih.gov/28382822

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