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2014 Fiscal Year Final Research Report

Single-molecule analysis of 1-nm stepping motion of linear motor carbohydrate hydrolase

Research Project

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Project/Area Number 24370062
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypePartial Multi-year Fund
Section一般
Research Field Biophysics
Research InstitutionOkazaki Research Facilities, National Institutes of Natural Sciences (2014)
The University of Tokyo (2012-2013)

Principal Investigator

IINO RYOTA  大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 教授 (70403003)

Co-Investigator(Kenkyū-buntansha) UCHIHASHI Takayuki  金沢大学, 数物科学系, 准教授 (30326300)
IGARASHI Kiyohiko  東京大学, 農学生命科学研究科, 准教授 (80345181)
Project Period (FY) 2012-04-01 – 2015-03-31
Keywords分子モーター / 1分子計測
Outline of Final Research Achievements

In this study, using single-molecule fluorescence microscopy and high speed atomic force microscopy, we determined kinetic constants of the elementary reaction steps for carbohydrate hydrolase TrCel7A against cellulose Iα and IIII. TrCel7A displayed similar binding and dissociation rate constants for cellulose Iα and IIII and similar fractions of productive binding on cellulose Iα and IIII. Furthermore, once productively bound, TrCel7A processively hydrolyzes and moves along cellulose Iα and IIII with similar translational rates. With structural models of cellulose Iα and IIII, we propose that different susceptibilities at high TrCel7A concentration arise from surface properties of substrate, including ratio of hydrophobic surface and number of available lanes.

Free Research Field

生物物理学

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Published: 2016-06-03  

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