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Enzyme activity usually correlates
Enzyme activity usually correlates with its conformational flexibility, such that higher flexibility(lower rigidity) is usually accompanied with higher activity. Tryptophan residues which emitfluorescence are most commonly located within the nonpolar interior environment of the proteins. Anexcellent way to experimentally determine the exposure of tryptophan residues to solution is bymeasuring the quenching (decrease) of their fluorescence. The effect of mutations on the accessibilityof tryptophan residues can be studied by measuring amount of fluorescence quenching by potassiumiodide (KI). Iodide ions selectively quench fluorescence emitted by exposed tryptophan residues.In the experiment whose results are presented below, fluorescence quenching on equal amounts ofthree mutated forms of an enzyme (mutant forms 1, 2, and 3) was measured after addition of variousconcentrations of KI (0–0.6 M). Excitation and emission wavelengths used were specific fortryptophan. Quenching data were analysed in terms of the Stern–Volmer constant, K SV , which can becalculated from the ratio of the unquenched and the quenched fluorescence intensities, F o /F, using therelationship
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酶活性通常与其构象柔韧性相关，因此较高的柔韧性<BR>（较低的刚性）通常伴随较高的活性。发出<BR>荧光的色氨酸残基最常见地位于蛋白质的非极性内部环境中。<BR>实验确定色氨酸残基暴露于溶液的一种极好的方法是通过<BR>测量其荧光的猝灭（降低）。突变对<BR>色氨酸残基可及性的影响可以通过测量<BR>碘化钾（KI）荧光猝灭的量来研究。碘离子选择性地抑制暴露的色氨酸残基发出的荧光。<BR>在下面显示结果的实验中，<BR>在添加各种<BR>浓度的KI（0–0.6 M）后，测量了等量三种突变形式的酶（突变形式1、2和3）的荧光猝灭。所用的激发和发射波长是<BR>色氨酸特有的。根据斯特恩-沃尔默常数K SV分析淬火数据，该常数可以<BR>使用以下<BR>关系式从非猝灭和猝灭荧光强度的比率F o / F计算得出
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酶活性通常与酶的构象灵活性相关，因此具有更高的灵活性<BR>（较低的刚度）通常伴随着较高的活动。发出色氨酸残留物<BR>荧光通常位于蛋白质的非极性内部环境中。通过实验确定色氨酸残留物暴露于溶液的极好方法<BR>测量荧光的淬火（减少）。突变对可访问性的影响<BR>通过测量钾的荧光淬火量，可以研究色氨酸残留物<BR>碘化物（KI）。碘离子选择性地淬火荧光由暴露的色氨酸残留物发出。<BR>在下面的实验中，荧光淬火在等量<BR>三种突变形式的酶（突变形式1，2和3）测量后，添加各种<BR>KI 浓度（0~0.6 M）。使用的激励和发射波长是特定<BR>色 氨 酸。根据斯特恩-沃尔默常数K SV对淬火数据进行了分析，该常数可以是<BR>根据未挤压和淬火荧光强度（F o /F）的比率计算，使用<BR>关系
正在翻译中..
Enzyme activity usually correlates with its conformational flexibility, such that higher flexibility(lower rigidity) is usually accompanied with higher activity. Tryptophan residues which emitfluorescence are most commonly located within the nonpolar interior environment of the proteins. Anexcellent way to experimentally determine the exposure of tryptophan residues to solution is bymeasuring the quenching (decrease) of their fluorescence. The effect of mutations on the accessibilityof tryptophan residues can be studied by measuring amount of fluorescence quenching by potassiumiodide (KI). Iodide ions selectively quench fluorescence emitted by exposed tryptophan residues.In the experiment whose results are presented below, fluorescence quenching on equal amounts ofthree mutated forms of an enzyme (mutant forms 1, 2, and 3) was measured after addition of variousconcentrations of KI (0–0.6 M). Excitation and emission wavelengths used were specific fortryptophan. Quenching data were analysed in terms of the Stern–Volmer constant, K SV , which can becalculated from the ratio of the unquenched and the quenched fluorescence intensities, F o /F, using therelationship<BR>
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