Structural analysis and molecular modeling of the RvH2-e functional unit of Rapana venosa hemocyanin

被引:3
作者
Velkova, Ludmila
Dolashka, Pavlina [1 ]
Dolashki, Aleksander [2 ]
Voelter, Wolfgang [2 ]
Atanasov, Boris
机构
[1] Bulgarian Acad Sci, Ctr Phytochem, Inst Organ Chem, BU-1113 Sofia, Bulgaria
[2] Univ Tubingen, Interfacultary Inst Biochem, D-72076 Tubingen, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2010年 / 1804卷 / 12期
关键词
Rapana venosa hemocyanin; Functional unit RvH2-e; Circular dichroism spectra; Reversible denaturation; Thermodinamic characteristics; Protein; 3D-structure; CARCINUS-AESTUARII HEMOCYANIN; KEYHOLE LIMPET HEMOCYANIN; SPECTROSCOPIC CHARACTERIZATION; CRYOELECTRON MICROSCOPY; HELIX-VULGARIS; SUBUNITS; STABILITY; EVOLUTION; PROTEINS;
D O I
10.1016/j.bbapap.2010.08.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Rapana venosa hemocyanin (RvH), a circulating glycoprotein of the marine snail, has a complex structure. To provide details on the stability of the protein, one functional unit, RvH2-e, was compared with the native molecule and the structural subunits, RvH1 and RvH2, via pH-T diagrams, typical phase portraits for stability and denaturation reversibility. By analyzing the T transition curves of RvH2-e at different pH values, several parameters of the thermodynamic functions were obtained. Increasing the temperature from 25 degrees C to 55 degrees C, the reversibility of the molecule of protein also increases, opening a reversibility window within the range of pH 4.0-8.0. On analyzing the pH transition curves, the start of the acid denaturation (below pH 6) and alkaline denaturation (above pH 9) was determined to be between 20 degrees C and 35 degrees C. For this range, the thermodynamic functions Delta H degrees and Delta G degrees for a standard temperature of 25 degrees C were calculated. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:2177 / 2182
页数:6
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