Export 35 results:
Author Title Type [ Year(Desc)]
Filters: Author is Udgaonkar, Jayant B  [Clear All Filters]
2016
Singh J, Udgaonkar JB.  2016.  The pathogenic mutation T182A converts the prion protein into a molten globule-like conformation whose misfolding to oligomers but not to fibrils is drastically accelerated.. Biochemistry. 55(3):459-69.
Sabareesan AThody, Singh J, Roy S, Udgaonkar JB, Mathew MK.  2016.  The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.. Biophys J. 110(8):1766-76.
Nussinov R, Udgaonkar JB.  2016.  Editorial overview: Folding and binding: Dynamic conformational heterogeneity is pivotal to cell life.. Curr Opin Struct Biol. 36:iv-vi.
Singh J, Udgaonkar JB.  2016.  Unraveling the Molecular Mechanism of pH-Induced Misfolding and Oligomerization of the Prion Protein.. J Mol Biol. 428(6):1345-55.
Goluguri RReddy, Udgaonkar JB.  2016.  Microsecond rearrangements of hydrophobic clusters in an initially collapsed globule prime structure formation during the folding of a small protein.. J Mol Biol.
Malhotra P, Udgaonkar JB.  2016.  Secondary Structural Change Can Occur Diffusely and Not Modularly during Protein Folding and Unfolding Reactions.. J Am Chem Soc. 138(18):5866-78.
Mondal S, Kallianpur MV, Udgaonkar JB, Krishnamoorthy G.  2016.  Molecular crowding causes narrowing of population heterogeneity and restricts internal dynamics in a protein. METHODS AND APPLICATIONS IN FLUORESCENCE. 4(1)
Malhotra P, Udgaonkar JB.  2016.  How cooperative are protein folding and unfolding transitions? Protein Sci.
Sabareesan AT, Udgaonkar JB.  2016.  Pathogenic mutations within the disordered palindromic region of the prion protein induce structure therein and accelerate the formation of misfolded oligomers.. J Mol Biol.
2017
Moulick R, Udgaonkar JB.  2017.  Identification and structural characterization of the precursor conformation of the prion protein which directly initiates misfolding and oligomerization.. J Mol Biol.
Sengupta I, Bhate SH, Das R, Udgaonkar JB.  2017.  Salt-mediated oligomerization of the mouse prion protein monitored by real time NMR.. J Mol Biol.
Nandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S.  2017.  Amino-acid composition after loop deletion drives domain swapping.. Protein Sci. 26(10)
Sen S, Goluguri RReddy, Udgaonkar JB.  2017.  A Dry Transition State More Compact Than the Native State Is Stabilized by Non-Native Interactions during the Unfolding of a Small Protein.. Biochemistry.
Aghera N, Udgaonkar JB.  2017.  Stepwise Assembly of β-Sheet Structure during the Folding of an SH3 Domain Revealed by a Pulsed Hydrogen Exchange Mass Spectrometry Study.. Biochemistry.
Sengupta I, Udgaonkar JB.  2017.  Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding.. Protein Expr Purif.
Kumar H, Singh J, Kumari P, Udgaonkar JB.  2017.  Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.. J Biol Chem.
Malhotra P, Jethva PN, Udgaonkar JB.  2017.  Chemical Denaturants Smoothen Ruggedness on the Free Energy Landscape of Protein Folding.. Biochemistry. 56(31):4053-4063.
Jethva PN, Udgaonkar JB.  2017.  Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant.. J Phys Chem B. 121(35):8263-8275.
Sabareesan AThody, Udgaonkar JB.  2017.  The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration.. Biochemistry. 56(44):5931-5942.