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Updated: May 24, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

一个未折叠的蛋白质的结构和动力学通过分子动力学模拟来检查

Kresten Lindorff-Larsen1, Nikola Trbovic, Paul Maragakis

  • 1D. E. Shaw Research, New York, New York 10036, USA. Kresten.Lindorff-Larsen@DEShawResearch.com

Journal of the American Chemical Society
|February 21, 2012
PubMed
概括

分子动力学模拟准确地捕捉了蛋白质乱. 对ACBP蛋白的200微秒模拟显示与NMR实验一致,进步了我们对内在无序蛋白质的理解.

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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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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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