Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures

Arteca GA.; Reimann CT.; Tapia O.; Velazquez I.

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Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures

机译：在真空中展开的溶菌酶折叠成天然的，准的和紧凑的结构

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We show that the relaxation dynamics of unfolded in vacuo lysozyme is not random. Analyses of molecular dynamics trajectories in a convenient space of molecular shape descriptors reveal a "favored" pattern of transitions leading to stable conformations. The relaxation paths exhibit a balanced change in shape features: globular spheroids are formed slowly enough to allow the proper entanglement of secondary-structural elements. The present study shows that a protein in vacuo can actually (re)fold into native and quasinative structures. The driving force for these transformations is intrinsic to the polypeptide chain. [S1063-651X(99)12605-9]. [References: 36]

机译：我们表明，在真空溶菌酶中展开的松弛动力学不是随机的。在分子形状描述子的便利空间中的分子动力学轨迹的分析揭示了导致稳定构象的转变的“有利”模式。弛豫路径在形状特征上表现出平衡的变化：球状球体的形成速度足够缓慢，以允许二级结构元素正确缠绕。本研究表明，真空中的蛋白质实际上可以（重新）折叠为天然和准结构。这些转化的驱动力是多肽链固有的。 [S1063-651X（99）12605-9]。 [参考：36]

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《Physical review, E. Statistical physics, plasmas, fluids, and related interdisciplinary topics》 |1999年第2期|共6页
作者
Arteca GA.; Reimann CT.; Tapia O.; Velazquez I.;
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正文语种 eng
中图分类物理学;
关键词
Molecular-dynamics simulations; Proteins in-vacuo; Disulfide-intact; Cytochrome-c; Gas-phase; Pathways; Conformations; Denaturation; Stability; Barriers;

机译：分子动力学模拟;真空中的蛋白质;完整的二硫键;细胞色素c;气相;途径;构象;变性;稳定性;障碍;

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1. Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures [J] . Arteca GA., Reimann CT., Tapia O., Physical review, E. Statistical physics, plasmas, fluids, and related interdisciplinary topics . 1999,第5aPta2期

机译：在真空中展开的溶菌酶折叠成天然的，准的和紧凑的结构
2. Relaxation dynamics of biopolymrs seeded with unfolded lysozyme transients in vacuo. The role of primary sequence in protein folding [J] . Gustavo A.Arteca, M.Paulino, C.T.Reimann, Physical chemistry chemical physics: PCCP . 2000,第22期

机译：在真空中接种了未折叠溶菌酶瞬变的生物多肽的松弛动力学。一级序列在蛋白质折叠中的作用
3. Transitions in Chain Entanglement and Compactness Associated with in Vacuo Unfolding of Lysozyme Ions [J] . Gustavo A.Arteca, C.T.Reimann, O.Tapia The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical . 2001,第21期

机译：溶菌酶离子的Vauo展开与链缠结和紧密度的转变
4. The kinetics of the folding/unfolding process of hydrated lysozyme studied by Nuclear Magnetic Resonance [C] . C. Corsaro, J. Spooren, N. Leone, International School of Physics "Enrico Fermi" . 2012

机译：核磁共振研究水合溶菌酶折叠/展开过程的动力学
5. Exploring the thermodynamics of the diversity of divalent magnesium ion interactions with native, partially folded, and unfolded RNA structures. [D] . Leipply, Desirae. 2010

机译：探索二价镁离子与天然，部分折叠和未折叠RNA结构相互作用的热力学。
6. Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme. [O] . M. E. Goldberg, Y. Guillou 1994

机译：天然的二硫键大大加速了溶菌酶折叠过程中二级结构的形成。
7. Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme. [O] . Goldberg, M. E., Guillou, Y. 2008

机译：天然的二硫键大大加速了溶菌酶折叠过程中二级结构的形成。

Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures

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