Swati Bandi, Ph.D.
Affiliations: | 2009 | Chemistry | University of Montana, Missoula, MT |
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"Swati Bandi"Mean distance: 8.05 | S | N | B | C | P |
Parents
Sign in to add mentor| Bruce Bowler | grad student | 2009 | Univ. Montana | |
| (Conformationally gated electron transfer studies of iso-1-cytochrome C.) | ||||
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Publications
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| Bandi S, Singh SM, Shah DD, et al. (2019) 2D NMR analysis of the effect of asparagine deamidation versus methionine oxidation on the structure, stability, aggregation, and function of a therapeutic protein. Molecular Pharmaceutics |
| Singh SM, Bandi S, Jones DNM, et al. (2017) Effect of Polysorbate 20 and Polysorbate 80 on the Higher Order Structure of a Monoclonal Antibody and its Fab and Fc Fragments Probed Using 2D NMR. Journal of Pharmaceutical Sciences |
| Singh SM, Bandi S, Mallela KMG. (2017) The N-terminal flanking region modulates the actin binding affinity of utrophin tandem calponin-homology domain. Biochemistry |
| Singh SM, Bandi S, Mallela KM. (2015) The N- and C-terminal domains differentially contribute to the structure and function of dystrophin and utrophin tandem calponin-homology (CH) domains. Biochemistry |
| Bandi S, Singh SM, Mallela KM. (2015) Interdomain Linker Determines Primarily the Structural Stability of Dystrophin and Utrophin Tandem Calponin-Homology Domains Rather than Their Actin-Binding Affinity. Biochemistry |
| McClelland LJ, Seagraves SM, Khan MK, et al. (2015) The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 805-19 |
| Bandi S, Bowler BE. (2015) Effect of an Ala81His mutation on the Met80 loop dynamics of iso-1-cytochrome c. Biochemistry. 54: 1729-42 |
| Singh SM, Bandi S, Shah DD, et al. (2014) Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. Plos One. 9: e110439 |
| Bandi S, Singh SM, Mallela KM. (2014) The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein. Biochemistry. 53: 2209-11 |
| Singh SM, Bandi S, Winder SJ, et al. (2014) The actin binding affinity of the utrophin tandem calponin-homology domain is primarily determined by its N-terminal domain. Biochemistry. 53: 1801-9 |