2011
DOI: 10.1134/s1995078011040082
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Study of characteristics of electrostatic interaction between RNases and mica surface using atomic force microscopy

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Cited by 3 publications
(7 citation statements)
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“…We have shown that binase much more effectively than pancreatic RNAse adsorbs on negatively charged substrate. The process of adsorption of RNAses depends on the distribution of charge on the surface of protein globule and is accompanied by aggregation of protein molecules [5]. The results presented in this work confirm our previous observations.…”
Section: Discussionsupporting
confidence: 82%
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“…We have shown that binase much more effectively than pancreatic RNAse adsorbs on negatively charged substrate. The process of adsorption of RNAses depends on the distribution of charge on the surface of protein globule and is accompanied by aggregation of protein molecules [5]. The results presented in this work confirm our previous observations.…”
Section: Discussionsupporting
confidence: 82%
“…This is most likely due to the higher polarity of RNAse A compared to binase. The dipole moments of RNAse A and binase are 545 D and 225 D, respectively 5 . The presence of high dipole moment, characterizing the skewness of a distribution of negative and positive charges in a protein molecule, determines the most probable spatial orientation of the dissolved protein molecules that are close to uncharged substrate surface.…”
Section: Discussionmentioning
confidence: 99%
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