SAWANO Masahide 澤野雅英

Researcher Number	10415177
Affiliation (based on the past Project Information) *help	2007: 独立行政法人理化学研究所, タンパク質結晶構造解析研究チーム, リサーチアソシエイト 2006: RIKEN, Protein Crystallographic Methodology Team, Research Associate, 構造解析高度化研究チーム, リサーチアソシエイト 2005: 独立行政法人理化学研究所, 横山構造分子生物学研究室, 協力研究員
Review Section/Research Field	Except Principal Investigator Structural biochemistry / Science and Engineering
Keywords	Except Principal Investigator NMR / 蛋白質の安定性 / 蛋白質のフォールディング / ピロリドンカルボキシペプチダーゼ / 超好熱菌 / Mutant Protein / Pyrrolidone Carboxyl Peptidase / α-Helix / Protein Stability / Hyperthermophile … More / Denatured Structure of a Protein / Protein Folding / 蛋白質の変異型 / CD / 蛋白質の変性 / アミノ酸変異型 / αヘリックス / 蛋白質の変性構造 / アミノ酸置換 / リアルタイム観察 / ピロリドンカルボキシペプチダーセ / フォールディングの律速 / 蛋白質の変性状態 / CutA1 / 熱安定性 / foldingの律速 / DSC Less

蛋白質フォールディングの律速のメカニズム
- Principal Investigator
  
  YUTANI Katsuhide
- Project Period (FY)
  2006 – 2007
- Research Category
  
  Grant-in-Aid for Scientific Research on Priority Areas
- Review Section
  
  Science and Engineering
- Research Institution
  The Institute of Physical and Chemical Research
Folding mechanism of a protein from a hyperthermophile with unusually slow folding rates
- Principal Investigator
  
  YUTANI Katsuhide
- Project Period (FY)
  2005 – 2006
- Research Category
  
  Grant-in-Aid for Scientific Research (C)
- Research Field
  
  Structural biochemistry
- Research Institution
  RIKEN

All 2008 2006 2005

All Journal Article

[Journal Article] Thermodynamic basis for the stabiities of three CutAls from Pyrococcus horikoshil, Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures2008
- Author(s)
  Masahide Sawano, et. al.
- Journal Title
  
  Biochemistry 47
  
  Pages: 721-730
- Peer Reviewed
- Data Source
  KAKENHI-PROJECT-18031043
[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006
- Author(s)
  澤野雅英, 油谷克英
- Journal Title
  
  Bionics[バイオニクス] No.24
  
  Pages: 68-69
- Data Source
  KAKENHI-PROJECT-17570102
[Journal Article] Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C2006
- Author(s)
  Tomoyuki Tanaka, Masahide Sawano, Kyoko Ogasahara, Yasushi Sakaguchi, Bagautdin Bagautdinov, Etsuko Katoh, Chizu Kuroishi, Akeo Shinkai, Shigeyuki Yokoyama, Katsuhide Yutani
- Journal Title
  
  FEBS Letters 580
  
  Pages: 4224-4230
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-17570102
[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006
- Author(s)
  澤野雅英, 油谷克英
- Journal Title
  
  Bionics[バイオニクス] No. 24
  
  Pages: 68-69
- Data Source
  KAKENHI-PROJECT-18031043
[Journal Article] Stabilization Mechanism of the Tryptophan Synthase α-Subunit from Thermus thermophilus HB8 : X-Ray Crystallographic Analysis and Calorimetry.2005
- Author(s)
  Yukuhiko Asada, Masahide Sawano, Kyoko Ogasahara, Junji Nakamura, Motonori Ota, Chizu Kuroishi, Mitsuaki Sugahara, Katsuhide Yutani, Naoki Kunishima
- Journal Title
  
  J. Biochem. 138
  
  Pages: 343-353
- NAID
  10017347311
- Description
  「研究成果報告書概要(欧文)」より
- Data Source
  KAKENHI-PROJECT-17570102

1. YUTANI Katsuhide (90089889)

# of Collaborated Projects: 2 results

# of Collaborated Products: 4 results
2. SEGAWA Shin-ichi (70103132)

# of Collaborated Projects: 2 results

# of Collaborated Products: 0 results

SAWANO Masahide 澤野雅英

Research Projects

Research Products

Co-Researchers

蛋白質フォールディングの律速のメカニズム

Principal Investigator

Project Period (FY)

Research Category

Review Section

Research Institution

Folding mechanism of a protein from a hyperthermophile with unusually slow folding rates

Principal Investigator

Project Period (FY)

Research Category

Research Field

Research Institution

[Journal Article] Thermodynamic basis for the stabiities of three CutAls from Pyrococcus horikoshil, Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures2008

Author(s)

Journal Title

Data Source

[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006

Author(s)

Journal Title

Data Source

[Journal Article] Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C2006

Author(s)

Journal Title

Description

Data Source

[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006

Author(s)

Journal Title

Data Source

[Journal Article] Stabilization Mechanism of the Tryptophan Synthase α-Subunit from Thermus thermophilus HB8 : X-Ray Crystallographic Analysis and Calorimetry.2005

Author(s)

Journal Title

NAID

Description

Data Source

SAWANO Masahide 澤野 雅英

Research Projects

Research Products

Co-Researchers

蛋白質フォールディングの律速のメカニズム

Principal Investigator

Project Period (FY)

Research Category

Review Section

Research Institution

Folding mechanism of a protein from a hyperthermophile with unusually slow folding rates

Principal Investigator

Project Period (FY)

Research Category

Research Field

Research Institution

[Journal Article] Thermodynamic basis for the stabiities of three CutAls from Pyrococcus horikoshil, Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures2008

Author(s)

Journal Title

Data Source

[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006

Author(s)

Journal Title

Data Source

[Journal Article] Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C2006

Author(s)

Journal Title

Description

Data Source

[Journal Article] 約150℃まで熱安定な超好熱菌由来のタンパク質2006

Author(s)

Journal Title

Data Source

[Journal Article] Stabilization Mechanism of the Tryptophan Synthase α-Subunit from Thermus thermophilus HB8 : X-Ray Crystallographic Analysis and Calorimetry.2005

Author(s)

Journal Title

NAID

Description

Data Source

SAWANO Masahide 澤野雅英