The Conformational State of Apomyoglobin in the Presence of Phospholipid Vesicles at Neutral pH

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• 作者：L. V. Basova ; E. I. Tiktopulo ; I. A. Kashparov and V. E. Bychkova
• 关键词：apomyoglobin ; phospholipid vesicles ; protein denaturation ; intermediate state
• 刊名：Molecular Biology
• 出版年：2004
• 出版时间：2004
• 年：2004
• 卷：38
• 期：2
• 页码：272-280
• 全文大小：72 KB
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Life Sciences
  Biochemistry
  Human Genetics
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3245

文摘

The conformational state of sperm whale apomyoglobin (apoMb) was studied at neutral pH in the presence of negatively charged vesicles using near and far UV circular dichroism, tryptophan fluorescence, differential scanning microcalorimetry, and fast performance liquid chromatography. Under these conditions, the apoMb structure undergoes transition from its native to an intermediate state. In this state the protein loses its rigid native structure but retains its secondary structure. However, the environment of tryptophan residues remains rather hydrophobic. This intermediate state of apoMb shows properties similar to those of its molten globule state in solution. It is shown that apoMb can bind to negatively charged phospholipid vesicles even at neutral pH. A possible functional role of this intermediate state is discussed.