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Updated: Jan 7, 2026

11:37
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
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分子ダイナミクスシミュレーションと主要成分分析による競争性ATPase阻害剤VER-155008によって誘発されるHsp70およびHsc70の分子阻害および構成変化を解明する
Maria Caroline Barbosa da Silva1, Carlos Gefferson Silva Falabelo2, Elvis Santos Leonardo3
1Laboratório de Simulação Computacional, Instituto de Biodiversidade, Universidade Federal do Oeste do Pará, Rua Vera Paz, Salé s/n, 68040-255 Santarém, Pará, Brazil.
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|January 5, 2026
まとめ
No abstract available in PubMed .
関連する概念動画
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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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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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