The fluorescence intensity decay of the single tryptophan residue, Trp-187, of free annexin V is described by the sum of three lifetime components (5.4, 1.3, and 0.4 ns), which may be correlated to three ground-state classes of Trp conformers. The two major classes (44 and 48%) are embedded in the protein matrix. When annexin V binds to calcium and liposomes made of dioleoylphosphatidylcholine and dioleoylphosphatidylserine, similar results are obtained whatever the (10-200) lipid ratio. The Trp fluorescence decay is fitted with only two components (6.9-7.2 and 2.0-2.2 ns). Decay-associated spectra reveal that the longest lifetime of bound annexin V can be related to Trp residues (60%) located in a partially polar environment, which could correspond to the protein-membrane interface. The shortest lifetime is attributed to Trp residues (40%) which reside in a hydrophobic surroundingthese Trp residues would penetrate into the phospholipid membrane and contribute to the stabilization of the 2D-array of annexin V molecules.

译文

游离膜联蛋白V的单个色氨酸残基Trp-187的荧光强度衰减由三个寿命成分(5.4、1.3和0.4 ns)的总和来描述,这三个成分可能与Trp构象异构体的三个基态类别相关。蛋白质基质中嵌入了两个主要类别(44%和48%)。当膜联蛋白V结合钙和由二油酰基磷脂酰胆碱和二油酰基磷脂酰丝氨酸制成的脂质体时,无论脂质比率为(10-200),都可获得相似的结果。 Trp荧光衰减仅适合两个分量(6.9-7.2和2.0-2.2 ns)。衰变相关光谱表明,结合的膜联蛋白V的最长寿命可能与位于部分极性环境中的Trp残基(60%)有关,这可能与蛋白质-膜界面相对应。最短的寿命归因于Trp残基(40%),该残基位于疏水的周围,这些Trp残基会渗入磷脂膜并有助于膜联蛋白V分子的2D阵列的稳定化。

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