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Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

机译：肌球蛋白部分折叠状态的结构和动态表征及其对蛋白质折叠的影响

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The structure and dynamics of two partially folded states of apomyoglobin have been characterized at equilibrium using multi-dimensional NMR spectroscopy. Residue-specific measurements of chemical shift and internal dynamics in these states and in the native apoprotein and holoprotein indicate progressive accumulation of secondary structure and increasing restriction of backbone dynamics as the chain collapses to form increasingly compact states. Under weakly folding conditions, the polypeptide fluctuates between unfolded states and local elements of structure that become extended and stabilized as the chain becomes more compact. These results provide a detailed model for molecular events that are likely to occur during folding of myoglobin. [References: 57]
机译：已使用多维NMR光谱在平衡状态下表征了血红蛋白球蛋白的两个部分折叠状态的结构和动力学。在这些状态以及天然脱辅基蛋白和全蛋白中，化学位移和内部动力学的残基特异性测量表明，随着链塌陷形成越来越紧凑的状态，二级结构的逐步积累和对主链动力学的限制越来越大。在弱折叠条件下，多肽在未折叠状态和结构的局部元件之间波动，该局部元件随着链变得更紧密而变得延伸和稳定。这些结果提供了在肌红蛋白折叠期间可能发生的分子事件的详细模型。 [参考：57]

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