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RISS 인기검색어
- 검색키워드
- 저자 : K. Alizadeh (검색결과 3 건)
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Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate
Ajloo, D.,Behnam, H.,Saboury, A.A.,Mohamadi-Zonoz, F.,Ranjbar, B.,Moosavi-Movahedi, A.A.,Hasani, Z.,Alizadeh, K.,Gharanfoli, M.,Amani, M. Korean Chemical Society 2007 Bulletin of the Korean Chemical Society Vol.28 No.5
The interaction of a polyoxometal (POM), K6SiW11Co(H2O)O39.10H2O (K6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (ν), lower Hill constant (n), higher binding constant (K), more negative entropy (ΔS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower Tm and Cp) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as Tm, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.
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Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate
D. Ajloo,H. Behnam,A. A. Saboury,F. Mohamadi-Zonoz,B. Ranjbar,A. A. Moosavi-Movahedi,Z. Hasani,K. Alizadeh,M. Gharanfoli,M. Amani 대한화학회 2007 Bulletin of the Korean Chemical Society Vol.28 No.5
The interaction of a polyoxometal (POM), K6SiW11Co(H2O)O39.10H2O (K6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (n), lower Hill constant (n), higher binding constant (K), more negative entropy (DS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower Tm and Cp) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as Tm, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.
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Lateral performance of CRCS connections with tube plate
Rahman Jafari,Nader K.A. Attari,Ali Nikkhoo,Saeid Alizadeh 국제구조공학회 2019 Steel and Composite Structures, An International J Vol.32 No.1
This paper presents experimental and analytical studies to evaluate the cyclic behaviour of Circular Reinforced Concrete column Steel beam (CRCS) connections. Two 3/4-scale CRCS specimens are tested under quasi-static reversed cyclic loading. Specimens were strengthened with a tube plate (TP) and a steel doubler plate (SDP). Furthermore; nine interior beam-through type RCS connections are simulated using nonlinear three-dimensional finite element method using ABAQUS software and are verified with experimental results. The results revealed that using the TP improves the performance of the panel zone by providing better confinement to the concrete. Utilizing the TP at the panel zone may absorb and distribute stress in this region. Results demonstrate that TP can be used instead of SDP. Test records indicate that specimens with TP, with and without SDP maintained their maximum strength up to 4% drift angle, satisfying the recommendation given by AISC341-2016 for composite special moment-resisting frames.
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