Light Scattering : a Novel Approach to Analyze Protein 4.1R FERM Domain Interaction with Inside-out-vesicles in Solution

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概要

• 論文の詳細を見る

著者

• Shiba Kohei

  Sysmex Corp.

• Nunomura Wataru

  Center For Geo-environmental Science Graduate School Of Engineering And Resource Science Akita University

関連論文

• 1P058 4.1R FERM domainのシー卜構造はアポカルモジュリンとの結合によって熱安定性を得る。(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)
• 2P-023 FT-IRを用いたカルモジュリンとペプチド複合体形成における二次構造の解析(蛋白質・構造(2),第46回日本生物物理学会年会)
• 2P081 Importance of b-sheet structure for heat stability of Ca^ saturated calmodulin : infrared spectroscopic analysis in physiological solution(30. Protein function (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
• 2P005 Fourier-transform infrared spectroscopic analysis of the calmodulin binding with peptides of protin 4.1R in physiological solution(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
• Light Scattering : a Novel Approach to Analyze Protein 4.1R FERM Domain Interaction with Inside-out-vesicles in Solution
• Light Scattering : a Novel Approach to Analyze Protein 4.1R FERM Domain Interaction with Inside-out-vesicles in Solution
• Bisphenol A Induces a Conformational Change in Protein Disulflde Isomerase

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