Yazar "Ozturk, Onur" seçeneğine göre listele

Listeleniyor 1 - 2 / 2
  • Küçük Resim Yok
    Öğe
    Molecular docking reveals fibrinogen binding sites on SARS-CoV-2 spike protein: A potential mechanism for COVID-19-related coagulation
    (2024) Ozturk, Onur; Kilinç, Evren; İrez, Batuhan Görkem; Timucin, Emel
    The Coronavirus Disease (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome coronavirus-2 (SARS-CoV-2), highlighted significant gaps in our understanding of the virus’s molecular structure, its biological properties, and the interactions between viral proteins and host biological systems, which have underscored the critical need for further research in this area. Coagulation disorders, particularly those leading to thromboinflammation, have been linked to severe complications in COVID-19 cases. The occurrence of thromboinflammation has likewise been corroborated in cases of both Severe Acute Respiratory Syndrome (SARS) and Middle East Respiratory Syndrome (MERS). In this study, we investigated the protein-protein interactions between the SARS-CoV-2 spike protein and fibrinogen, a glycoprotein that plays a crucial role in blood coagulation. Molecular docking analysis revealed key interactions between the ? and ? subunits of fibrinogen and the spike protein. The findings suggest that these interactions may contribute to the understanding of the coagulation disorders observed in COVID-19 patients. This study provides insights into the molecular mechanisms underlying these disorders and identifies potential targets for the development of therapeutic interventions.
  • Küçük Resim Yok
    Öğe
    Protein structure analysis of abnormal hemoglobins; Hb D-Los Angeles, Hb S and Hb G-Coushatta
    (2024) Ozturk, Onur
    Computational methods have been extensively utilized for protein structure prediction and modeling, including hemoglobin. These methods have provided valuable insights into the three-dimensional conformation of hemoglobin, its allosteric regulation, and its oxygen-binding capacity. For instance, computational modeling has been employed to understand the structural mechanism of hemoglobin, shedding light on the equilibrium between alternative structures, like the tense (T) and relaxed (R) states, which influence oxygen affinity and binding. Abnormal hemoglobins are associated with various genetic and clinical implications. The mutations in the globin genes to cause changes in the molecular structure of hemoglobin, affecting its biological properties such as oxygen carrying capacity and stability. RMSD is the mean displacement of atoms or molecular structures. Therefore, RMSD is a preferred parameter in structural similarity modeling studies. RMSD values calculated for pairwise protein structures are Hb A (Normal Hb)-Hb D-Los Angeles 3.44 Å, Hb A-Hb S 3.339 Å, Hb A-Hb G-Coushatta 3.35 Å. The aim of this study is to discuss the possible structural and electrical properties of abnormal haemoglobin molecules using protein modelling.