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

Trp-187,游离膜联蛋白V的单个色氨酸残基的荧光强度衰减由三个寿命分量 (5.4、1.3和0.4 ns) 的总和描述,这可能与Trp构象的三个基态类别相关。两个主要类别 (44和48%) 嵌入蛋白质基质中。当膜联蛋白V与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结合时,无论 (10-200) 脂质比率如何,都获得相似的结果。Trp荧光衰减仅适合两种组分 (6.9-7.2和2.0-2.2 ns)。衰变相关光谱表明,结合膜联蛋白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,这可能对应于蛋白质-膜界面。最短的寿命归因于存在于疏水性周围的Trp残基 (40%),这些Trp残基会渗透到磷脂膜中,并有助于膜联蛋白V分子的2d阵列的稳定。

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