Intrinsic dynamics of an enzyme underlies catalysis

被引：0

作者：

Elan Z. Eisenmesser

Oscar Millet

Wladimir Labeikovsky

Dmitry M. Korzhnev

Magnus Wolf-Watz

Daryl A. Bosco

Jack J. Skalicky

Lewis E. Kay

Dorothee Kern

机构：

[1] Brandeis University,Department of Biochemistry, Howard Hughes Medical Institute

[2] University of Toronto,Departments of Medical Genetics, Biochemistry and Chemistry

[3] National High Magnetic Field Laboratory at Florida State University,Plataforma de Biomolecules

[4] Parc Cientific de Barcelona,Department of Biochemistry

[5] The Scripps Research Institute,Department of Biochemistry

[6] Department of Chemistry,undefined

[7] University of Utah School of Medicine,undefined

[8] University of Umeå,undefined

来源：

Nature | 2005年 / 438卷

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摘要：

Here's a new way to look at familiar enzymes. A new technology that can detect ultra-rare states of a protein (cyclophilin A in this instance) shows that rather than having a range of conformations to which it resorts during catalysis, it has them all before it starts. Protein motions needed for catalysis are intrinsic to the enzyme and take in the whole molecule, not just the traditional centre of attention, the active site.

引用

页码：117 / 121

页数：4

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