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Loosening of the phage structure in a low ionic strength environment
Authors:Gy Rontó  K Tóth  G Csik  L A Feigin  D T Svergun  A T Dembo  E V Shtikova
Institution:(1) Institute of Biophysics, Semmelweis Medical University, P.O.B. 263, H-1444 Budapest, Hungary;(2) Institute of Crystallography, Academy of Sciences of the USSR, Leninsky prospect 59, SU-117333 Moscow, USSR;(3) Institute of Haematology and Blood Transfusion, Nov Zykovsky prospect 4a, SU-125167 Moscow, USSR
Abstract:Structural parameters of phage T7 were compared in two frequently use Tris buffers of high and low ionic strength, in order to explain the different biological activity and drug-binding characteristics.Characteristics of the whole phage geometry were obtained by viscosimetry, static and quasi-elastic light-scattering and small-angle X-ray scattering. The latter method revealed dissimilarities in the intraphage DNA compactness, consistent with the findings of the optical absorption melting studies.Alterations in the particle dimensions determined in the same sample by different methods are discussed, and a model is constructed to explain the structural modifications that occur on lowering the ionic strength.
Keywords:Nucleoprotein structure  small-angle X-ray scattering  light-scattering
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