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Updated: Jul 19, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

ベータヘアピン折り畳みの自由エネルギー景観は,平行テンプレートとメタダイナミクスの組み合わせによるものです

Giovanni Bussi1, Francesco Luigi Gervasio, Alessandro Laio

  • 1Computational Science, Department of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zürich, c/o USI Campus, Via Buffi 13, CH-6900 Lugano, Switzerland. gbussi@ethz.ch

Journal of the American Chemical Society
|October 13, 2006
PubMed
まとめ

私たちは,パラレルテンピングとメタダイナミクスを組み合わせた新しい自由エネルギー計算方法を開発しました. このアプローチは,明示的な水中のベータヘアピン折り畳みのための高自由エネルギー領域のサンプリングを強化します.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Protein Folding01:25

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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Protein Folding01:22

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Gibbs Free Energy02:39

Gibbs Free Energy

One of the challenges of using the second law of thermodynamics to determine if a process is spontaneous is that it requires measurements of the entropy change for the system and the entropy change for the surroundings. An alternative approach involving a new thermodynamic property defined in terms of system properties only was introduced in the late nineteenth century by American mathematician Josiah Willard Gibbs. This new property is called the Gibbs free energy (G) (or simply the free...
Arrhenius Plots02:34

Arrhenius Plots

The Arrhenius equation relates the activation energy and the rate constant, k, for chemical reactions. In the Arrhenius equation, k = Ae−Ea/RT, R is the ideal gas constant, which has a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is a constant called the frequency factor, which is related to the frequency of collisions and the orientation of the reacting molecules.
The Arrhenius equation can be used to...