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Updated: May 24, 2025

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

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在无序蛋白质模拟中,从能量陷中解开折叠

Jeffrey M Lotthammer1,2, Alex S Holehouse1,2

  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States.

Journal of chemical information and modeling
|March 5, 2025
PubMed
概括

我们开发了一种新的算法,用于在模拟中量化蛋白质结构异质性. 这种方法准确地评估了内在无序蛋白质 (IDP) 的采样,确保了可靠的模拟结果.

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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments09:25

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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

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Molecular Chaperones and Protein Folding

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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Noncovalent Attractions in Biomolecules

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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