Cargando…
Size-Dependent Interplay of Volume Exclusion Versus Soft Interactions: Cytochrome c in Macromolecular Crowded Environment
Even though there are a great number of possible conformational states, how a protein generated as a linear unfolded polypeptide efficiently folds into its physiologically active form remained a fascinating and unanswered enigma inside crowded conditions of cells. In this study, various spectroscopi...
Autores principales: | Parray, Zahoor Ahmad, Ahmad, Faizan, Chaudhary, Anis Ahmad, Rudayni, Hassan Ahmad, Al-Zharani, Mohammed, Hassan, Md. Imtaiyaz, Islam, Asimul |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9174945/ https://www.ncbi.nlm.nih.gov/pubmed/35693552 http://dx.doi.org/10.3389/fmolb.2022.849683 |
Ejemplares similares
-
Measuring Structural Changes in Cytochrome c under Crowded Conditions Using In Vitro and In Silico Approaches
por: Parray, Zahoor Ahmad, et al.
Publicado: (2022) -
Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder
por: Shahid, Sumra, et al.
Publicado: (2019) -
Interaction of polyethylene glycol with cytochrome c investigated via in vitro and in silico approaches
por: Parray, Zahoor Ahmad, et al.
Publicado: (2021) -
Structural Refolding and Thermal Stability of Myoglobin in the Presence of Mixture of Crowders: Importance of Various Interactions for Protein Stabilization in Crowded Conditions
por: Parray, Zahoor Ahmad, et al.
Publicado: (2021) -
Effects of Ethylene Glycol on the Structure and Stability
of Myoglobin Using Spectroscopic, Interaction, and In Silico Approaches: Monomer Is Different from Those of Its Polymers
por: Parray, Zahoor Ahmad, et al.
Publicado: (2020)