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Bhanu Pratap Singh
Researcher at University of Hyderabad
Publications - 9
Citations - 121
Bhanu Pratap Singh is an academic researcher from University of Hyderabad. The author has contributed to research in topics: Chaperone (protein) & Isothermal titration calorimetry. The author has an hindex of 5, co-authored 9 publications receiving 83 citations. Previous affiliations of Bhanu Pratap Singh include University of Edinburgh.
Papers
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Journal ArticleDOI
Isothermal titration calorimetric studies on the interaction of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes.
TL;DR: The interaction of the major bovine seminal plasma protein, PDC-109 with lipid membranes was investigated by isothermal titration calorimetry, and entropically driven binding process indicates that hydrophobic interactions play a major role in the overall binding process.
Journal ArticleDOI
HSP-1/2, a major protein of equine seminal plasma, exhibits chaperone-like activity.
TL;DR: It is demonstrated that HSP-1/2 functions as a molecular chaperone in vitro, and it is suggested that it may protect other proteins of equine seminal plasma from unfolding/misfolding or aggregation.
Journal ArticleDOI
Glycosylation differentially modulates membranolytic and chaperone-like activities of PDC-109, the major protein of bovine seminal plasma.
Bhanu Pratap Singh,Rajeshwer S. Sankhala,Abhishek Asthana,Tangirala Ramakrishna,Ch. Mohan Rao,Musti J. Swamy +5 more
TL;DR: Differential modulation of the membrane-perturbing and chaperone-like activities has been explained on the basis of higher membrane-penetrating ability and lower solubility of glycan-lacking BSP-A2 as compared to the glycosylated B SP-A1.
Journal ArticleDOI
Spermine and spermidine act as chemical chaperones and enhance chaperone-like and membranolytic activities of major bovine seminal plasma protein, PDC-109.
TL;DR: Results indicate that at the high concentrations present in the seminal plasma spermine/spermidine exhibit a positive modulatory effect on the chaperone-like activity of PDC-109 and may also function as chemical chaperones and protect other seminal plasma proteins from various kinds of stress.
Book ChapterDOI
Factors Influencing the Chaperone-Like Activity of Major Proteins of Mammalian Seminal Plasma, Equine HSP-1/2 and Bovine PDC-109: Effect of Membrane Binding, pH and Ionic Strength.
TL;DR: Results indicate that hydrophobicity and polydispersity are important for the chaperone-like activity of HSP-1/2 and factors that can alter these properties of H SP- 1/2 can modulate its CLA.