[The heat denaturation of bacterial ribonuclease studied by infrared spectroscopy].

E A Strupishina
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Abstract

The thermal denaturation of bacterial ribonuclease in the interval of pH 2.5-7.0 has been investigated by means of infra-red spectroscopy method. The protein melting for pH 2.5 begins at the temperature 25 degrees C and is accompanied by secondary protein structure reconstruction, partially destroying native beta-structure and leading to new denatured conformation appearance of different types of beta-turns. Spectral changes for pH 3.5 and 7.0 are significantly less in the same frequency areas. At the temperature more than 50 degrees C protein aggregation takes place with inter-molecule-beta-form formation.

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[用红外光谱研究细菌核糖核酸酶的热变性]。
用红外光谱法研究了细菌核糖核酸酶在pH 2.5 ~ 7.0范围内的热变性。pH值为2.5的蛋白质熔化始于25℃,并伴随着蛋白质的二级结构重建,部分破坏了天然的β结构,导致不同类型β转的新变性构象外观。pH值为3.5和7.0时,在相同频率区域的光谱变化明显较小。在50摄氏度以上的温度下,蛋白质聚集以分子间β形式形成。
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