関連する実験動画

Updated: Jun 8, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

タンパク質の構造ダイナミクスの原子レベルでの特徴付け

David E Shaw1, Paul Maragakis, Kresten Lindorff-Larsen

  • 1D. E. Shaw Research, 120 West 45th Street, New York, NY 10036, USA. David.Shaw@DEShawResearch.com

Science (New York, N.Y.)
|October 16, 2010
PubMed
まとめ

極めて長い分子動力学 (MD) シミュレーションにより,タンパク質の折り畳み経路と構造変化が明らかになった. これらのシミュレーションは,生物学的に関連する時間スケールでのタンパク質動力学に関する新しい洞察を提供します.

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Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Protein Organization01:13

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Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.