A
Avanish S. Parmar
Researcher at Indian Institute of Technology (BHU) Varanasi
Publications - 52
Citations - 825
Avanish S. Parmar is an academic researcher from Indian Institute of Technology (BHU) Varanasi. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 14, co-authored 38 publications receiving 560 citations. Previous affiliations of Avanish S. Parmar include University of Hyderabad & University of South Florida.
Papers
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Journal ArticleDOI
Hydration and Hydrodynamic Interactions of Lysozyme: Effects of Chaotropic versus Kosmotropic Ions
Avanish S. Parmar,Martin Muschol +1 more
TL;DR: The protein hydration shell is more resistant than bulk water to changes in its local structure by either chaotropic or kosmotropic ions, infer that the proteinHydrodynamic protein interactions changed from attractive to repulsive, i.e., in exact opposition to salt-induced changes in direct protein interactions.
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Pre-assembled clusters distort crystal nucleation kinetics in supersaturated lysozyme solutions
TL;DR: It is found that commercial sources of lyophilized hen-egg white lysozyme used in nucleation studies contain significant populations of large, pre-assembled lyso enzyme clusters that act as heterogeneous nucleation centers that enhance the rate of crystal nucleation and significantly deteriorate the quality of macroscopic crystals.
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Self-Assembly of Left- and Right-Handed Molecular Screws
Fei Xu,I. John Khan,Kenneth N. McGuinness,Avanish S. Parmar,Teresita Silva,N. Sanjeeva Murthy,Vikas Nanda +6 more
TL;DR: A geometric ridges-in-grooves model of interacting helices indicates that heterochiral associations should generally be favored in this class of structures, and tested this principle using a collagen peptide triple-helix.
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Circular Dichroism Spectroscopy of Collagen Fibrillogenesis: A New Use for an Old Technique
TL;DR: It is demonstrated that CD spectroscopy, a technique used primarily to evaluate the secondary structure of proteins, can also be employed to monitor collagen fibrillogenesis, and identified a unique fibril spectrum distinct from triple helix and random coil conformations.
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Methacrylation Induces Rapid, Temperature-Dependent, Reversible Self-Assembly of Type-I Collagen
Kathryn E. Drzewiecki,Avanish S. Parmar,Ian D. Gaudet,Jonathan R. Branch,Douglas H. Pike,Vikas Nanda,David I. Shreiber +6 more
TL;DR: It is demonstrated that structural reversibility is manifest across multiple scales from the protein topology of the triple helix up through the rheological properties of the CMA hydrogel, which makes CMA a powerful model for studying the complex process of hierarchical collagen self-assembly.