Jethva, P. and Udgaonkar, J. B. (2017)
Modulation of the Extent of Cooperative Structural Change During Protein Folding by Chemical Denaturant
J. Phys. Chem. B., 121, 8263-8275

Kumar, H., Singh, J., Kumari, P. and Udgaonkar, J. B. (2017)
Modulation of the extent of structural heterogeneity in alpha-synuclein fibrils by the small molecule thioflavin T
J. Biol. Chem. (In press)

Sengupta, I. and Udgaonkar, J. B. (2017)
Expression and purification of single cysteine containing mutant variants of the mouse prion protein by oxidative refolding
Protein. Expr. Purif. 140, 1-7

Malhotra, P., Jethva, P.N. and Udgaonkar, J.B. (2017)
Chemical denaturants smoothen ruggedness on the free energy landscape of protein folding
Biochemistry 56, 4053−4063

Nandwani, N., Surana, P., Udgaonkar, J. B., Das, R. and Gosavi, S. (2017)
Prot. Sci. (In press)

Aghera, N. and Udgaonkar, J. B. (2017)
Biochemistry 56, 3754−3769

Sengupta, I., Bhate, S. H., Das. R. and Udgaonkar, J. B. (2017)
J. Mol. Biol. 429, 1852-1872

Moulick, R. and Udgaonkar, J. B. (2017)
J. Mol. Biol. 429, 886-899

Sabareesan A. T. and Udgaonkar, J. B. (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., 428, 3935-3947

Malhotra, P. and Udgaonkar, J. B. (2016)
How cooperative are protein folding and unfolding transitions?
Protein Sci., 25, 1924-1941

Goluguri R. and Udgaonkar, J. B. (2016)
Microsecond rearrangements of hydrophobic clusters in an initially collapsed globule prime structure formation during the folding of a small protein.
J. Mol. Biol., 428, 3102-3117

Malhotra P. and Udgaonkar, J. B. (2016)
Secondary structural change can occur diffusely and not modularly during protein folding and unfolding reactions.
J. Am. Chem. Soc., 138, 5866-5878

Sabareesan, A. T., Singh, J., Roy, S., Udgaonkar, J. B. and Mathew, M. K. (2016)
The pathogenic A116V mutation enhances the selective ion-channel activity of the prion protein in artificial and living cell membranes.
Biophys. J., 110, 1766-1776

Nussinov, R. and Udgaonkar, J.B. (2016)
Folding and binding: dynamic conformational heterogeneity is pivotal to cell life.
Curr. Opin. Struct. Biol., 36, 4-6

Singh, J. and Udgaonkar, J.B (2016)
Unraveling the molecular mechanism of pH-induced misfolding and oligomerization of the prion protein.
J. Mol. Biol., 428, 1345-1355

Singh, J. and Udgaonkar, J.B (2016)
The pathogenic mutation T182A converts the prion protein into a molten globult-like conformation whose misfolding to oligomers but not to fibrils is drastically accelerated.
Biochemistry , 55, 459-469

Mondal, S., Kallianpur, M.V., Udgaonkar, J. B. and Krishnamoorthy, G. (2015)
Molecular crowding causes narrowing of population heterogeneity and restricts internal dynamics in a protein
Methods and Applications in Fluorescence 4, 014003

Moulick, R., Das, R. and Udgaonkar, J. B. (2015)
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR
J. Biol. Chem., 290, 25227-25240

Goluguri, R. and Udgaonkar, J. B. (2015)
Rise of the helix from a collapsed globule during the folding of monellin
Biochemistry 54, 5356-5365

Singh, J. and Udgaonkar, J. B. (2015)
Molecular mechanism of the misfolding and oligomerization of the prion protein: current understanding and its implications
Biochemistry 54, 4431-4442

Malhotra, P. and Udgaonkar, J. B. (2015)
Tuning cooperativity on the free energy landscape of protein folding
Biochemistry 54, 3431-3441

Singh, J. and Udgaonkar, J. B. (2015)
Structural Effects of Multiple Pathogenic Mutations Suggest a Model for the Initiation of Misfolding of the Prion Protein
Angew. Chem. Int. Ed. ,54, 7529-7533

Milan-Garces, E., Thaore, P., Udgaonkar, J.B. and Puranik, M. (2015)
Formation of a CH-πContact in the Core of Native Barstar during Folding.
J. Phys. Chem B. , 119, 2928-2932

Singh, J., Kumar, H., Sabareesan, A. T. and Udgaonkar, J. B. (2014)
Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerization
J. Am. Chem. Soc. 136, 16704-16707

Ramachandran, G., Milan-Garces, E., Udgaonkar, J.B. and Puranik, M. (2014)
Resonance Raman Spectroscopic Measurements Delineate the Structural Changes that occur during Tau Fibril Formation
Biochemistry, 53, 6550−6565

Milan-Garces, E.A., Mondal, S., Udgaonkar, J.B. and Puranik, M. (2014)
Intricate packing in the hydrophobic core of barstar through a CH-Pi Interaction
J. Raman Spectros., 45, 814-821

Malhotra, P. and Udgaonkar, J.B. (2014)
High energy intermediates in protein unfolding characterized by thiol labeling under native-like conditions
Biochemistry, 53, 3608-3620

Bhardwaj, V., Panicker, M. and Udgaonkar, J.B. (2014)
Fluorescence anisotropy uncovers changes in protein packing with inclusion growth in a cellular model of poly-glutamine aggregation
Biochemistry, 53, 3621-3636

Dasgupta, A., Udgaonkar, J.B. and Das, P. (2014)
Multistage Unfolding of a SH3 Domain: An Initial Urea-Filled Dry Molten Globule Precedes a Wet Molten Globule with Non-Native Structure
J. Phys. Chem. B, 118, 6380-6392

Sabareesan, A.T. and Udgaonkar, J.B. (2014)
Amyloid fibril formation by the chain B subunit of monellin occurs by a nucleation dependent polymerization mechanism
Biochemistry, 53, 1206-1217

Moulick, R. and Udgaonkar, J.B. (2014)
Thermodynamic Characterization of the Unfolding of the Prion Protein
Biophys J., 106, 410-420

Kishore, M., Krishnamoorthy, G. and Udgaonkar, J.B. (2013)
Critical evaluation of the two-state model describing the equilibrium unfolding of the PI3K SH3 domain by time-resolved fluorescence resonance energy transfer
Biochemistry, 52, 9482-9496

Ramachandran, G. and Udgaonkar, J.B. (2013)
Difference in fibril core stability of two tau four repeat domain proteins: A hydrogen-deuterium exchange coupled to mass spectrometry study.
Biochemistry, 52, 8787-8789

Sarkar, S.S., Udgaonkar, J.B. and Krishnamoorthy, G. (2013)
Unfolding of a small protein proceeds through dry and wet globules and a solvated transition state.
Biophys J., 105, 2392-2402

Aghera, N. and Udgaonkar, J.B. (2013)
The utilization of competing unfolding pathways of monellin is dictated by enthalpic barriers.
Biochemistry, 52, 5770-5779

Singh, J. and Udgaonkar, J.B. (2013)
Dissection of conformational conversion events during prion amyloid fibril formation using hydrogen exchange and mass spectrometry
J. Mol. Biol., 425, 3510-3521

Ramachandran, G. and Udgaonkar, J.B. (2013)
Mechanistic studies unravel the complexity inherent in tau aggregation leading to Alzheimer's disease and the tauopathies
Biochemistry, 52, 4107-4126

Udgaonkar, J.B. and Marqusee, S. (2013)
Folding and Binding
Curr. Opin. Struct. Biol., 23, 1-3

Udgaonkar, J.B. (2013)
Polypeptide chain collapse and protein folding
Arch. Biochem. Biophys., 531, 24-33

Aghera, N., Dasgupta, I., and Udgaonkar, J.B. (2012)
A buried ionizable residue destabilizes the native state and the transition state in the folding of monellin
Biochemistry, 51, 9058−9066

Dasgupta, A. and Udgaonkar, J.B. (2012)
Transient non-native burial of a Trp residue occurs initially during the unfolding of a SH3 domain
Biochemistry 51, 8226-8234

Jha, A., Udgaonkar, J.B. and Krishnamoorthy, G. (2012)
Solvent-Induced Tuning of Internal Structure in a Protein Amyloid protofibril
Biophys. J. ,103, 797-806

Singh, J., Sabareesan, A.T., Mathew, M.K., and Udgaonkar, J.B. (2012)
Development of the structural core and of conformational heterogeneity during the conversion of oligomers of the mouse prion protein to worm like amyloid fibrils.
J. Mol. Biol. 423, 217-231

Aghera, N. and Udgaonkar, J.B. (2012)
Kinetic studies of the folding of heterodimeric monellin: evidence for switching between alternative parallel pathways
J. Mol. Biol. ,420, 235-250

Dasgupta, A. and Udgaonkar, J.B. (2012)
Four state folding of a SH3 domain: salt-induced modulation of the stabilities of the intermediates and native state
Biochemistry 51, 4723-4734

Jha, S.K. , Deepalakshmi, P.D. and Udgaonkar, J.B. (2012)
Characterization of Deamidation of Barstar using Electrospray Ionisation Quadruple Time of Flight Mass Spectrometry, which stabilizes an Equilibrium Unfolding Intermediate
Prot.Sci., 21, 633-646

Ramachandran, G. and Udgaonkar, J.B. (2012)
Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau
J. Mol. Biol. 421, 296-314

Wani, A.H. and Udgaonkar, J.B. (2012)
Mass spectrometry studies of protein folding
Curr. Sci., 102,1-21

Jain, S. and Udgaonkar, J.B. (2011)
Prion Protein Aggregation
Curr. Sci., 101,1311-1327

Ramachandran, G. and Udgaonkar, J.B. (2011)
Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by tau
J. Biol. Chem., 286, 38948-38959

Sarkar, S.S., Udgaonkar, J.B. and Krishnamoorthy, G. (2011)
Reduced Fluorescence Lifetime Heterogeneity of 5-Fluorotryptophan in Comparison to Tryptophan in Proteins: Implication for Resonance Energy Transfer Experiments
J. Phys. Chem B., 115, 7479-7486

Jha, S.K., Dasgupta, A., Malhotra, P. and Udgaonkar, J.B. (2011)
Identification of multiple folding pathways of monellin using pulsed -thiol labeling and mass spectrometry
Biochemistry, 50, 3062-3074

Aghera, N., Earanna, N. and Udgaonkar, J.B. (2011)
Equilibrium unfolding studies of monellin: the double chain variant appears more stable than the single chain variant
Biochemistry, 50, 2434-2444

Jain, S. and Udgaonkar, J.B. (2011)
Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions
Biochemistry, 50, 1153-1161

Sekhar, A. and Udgaonkar, J.B. (2011)
Fluoroalcohol-induced Modulation of the Pathway of Amyloid Protofibril Formation by Barstar
Biochemistry, 50, 805-819

Jha, A., Ishii, K., Udgaonkar, J.B., Tahara, T. and Krishnamoorthy, G. (2011)
Exploration of the correlation between solvation dynamics and internal dynamics of a protein
Biochemistry, 50, 397-408

Aghera, N. and Udgaonkar, J.B. (2011)
Heterologous expression, purification and characterization of heterodimeric monellin
Prot. Expr. Pur.,76, 248-253

Dasgupta A. and Udgaonkar, J.B. (2010)
Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase
J. Mol. Biol., 403, 430-445

Jain, S. and Udgaonkar, J.B. (2010)
Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein
Biochemistry, 49, 7615-7624

Jha, S.K. and Udgaonkar, J.B. (2010)
Free energy barriers in protein folding and unfolding
Curr. Sci., 99, 457-475

Kumar, S. and Udgaonkar, J.B. (2010)
Mechanisms of amyloid fibril formation by proteins
Curr. Sci., 96,1053-1070

Wani, A.H. and Udgaonkar, J.B. (2009)
Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.
Proc. Natl. Acad. Sci. USA, 106, 20711-20716

Jha, A., Udgaonkar, J.B. and Krishnamoorthy, G. (2009)
Characterization of the heterogeneity and specificity of inter-polypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics.
J. Mol. Biol. 393, 735-752

Kumar, S. and Udgaonkar J.B. (2009)
Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein.
Biochemistry, 48, 6441-6449

Jha, S.K. and Udgaonkar, J.B. (2009)
Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.
Proc. Natl. Acad. Sci. USA, 106, 12289-12294

Jha, S.K., Dhar, D., Krishnamoorthy, G. and Udgaonkar, J.B.(2009)
Continuous dissolution of structure during the unfolding of a small protein.
Proc. Natl. Acad. Sci. USA, 106, 11113-1118

Patra, A.K. & Udgaonkar, J. B. (2009)
GroEL can unfold late intermediates populated on the folding pathways of monellin.
J. Mol. Biol. 389, 759-775

Sinha, K. K. and Udgaonkar, J. B. (2009)
Early Events in Protein Folding.
Curr. Sci. Vol. 96, No. 8, 1053-1070

Wani, A. H. and Udgaonkar, J. B. (2009)
Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
J. Mol. Biol. 387, 348-362

Kumar S. & Udgaonkar, J.B. (2009)
Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation.
J. Mol. Biol. 385, 1266-1276

Beena K., Kulothungan, R., Patra, A.K., Udgaonkar, J.B. & Varadarajan, R. (2009)
SecB mediated protein export need not occur via kinetic partitioning.
J. Mol. Biol. 385, 1243-1256

Jain, S. & Udgaonkar, J.B. (2008)
Evidence for step-wise formation of amyloid fibrils by the mouse prion protein.
J. Mol. Biol. 382, 1228-1241

Udgaonkar, J.B. (2008)
Multiple routes and structural heterogeneity in protein folding.
Annual Reviews of Biophysics. 37, 489-510

Sinha, K.K. & Udgaonkar, J.B. (2008)
Barrier-less evolution of structure during the sub-ms folding reaction of a small protein.
Proc. Natl. Acad. Sci. USA,105, 7998-8003

Jha, S.K. and Udgaonkar, J.B. (2007)
Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry.
J. Biol. Chem 2007,Vol. 282, No.52,37479-37491

Patra, A.K. and Udgaonkar, J.B. (2007)
Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
Biochemistry, 46, 11727-11743

Sinha, K.K. & Udgaonkar, J.B. (2007)
Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements.
J. Mol. Biol., Vol. 370, No. 2, 385-405

Saxena, A.M., Krishnamoorthy, G., Udgaonkar, J.B. and Periasamy, N. (2007)
Identification of intermediate species in protein folding by quantitative analysis of amplitudes in time-domain fluorescence spectroscopy.
J. Chem Sci., Vol.119 No.2, 61-69

Kumar, S., Mohanty, S.K. & Udgaonkar, J.B. (2007)
Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion
J. Mol. Biol. 2007, 367, No. 4, 1186-1204

Pradeep, L. & Udgaonkar, J.B. (2006)
Diffusional barrier in the unfolding of a small protein.
J. Mol. Biol. 2006, 366, No 3, 1016-1028

Wani, A. H. & Udgaonkar, J. B. (2006).
HX-ESI-MS and Optical Studies of the Unfolding of Thioredoxin Indicate Stabilization of a Partially Unfolded, Aggregation-Competent Intermediate at Low pH.
Biochemistry, 2006, 45, 11226-11238

Saxena, A.M., Udgaonkar, J.B. & Krishnamoorthy, G. (2006).
Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure.
J. Mol. Biol. 2006, 359, 174-189

Mukhopadhyay, S, Nayak, P, Udgaonkar, JB and Krishnamoorthy, G. (2006).
Characterization of the Formation of Amyloid Protofibrils from Barstar by Mapping Residue-Specific Fluorescence Dynamics.
J. Mol. Biol. 2006, 358, 935-942

Sinha, K.K. & Udgaonkar, J.B.
Dependence of the size of the initially collapsed form during the folding of barstar on denaturant concentration: evidence for a continuous transition.
J. Mol. Biol. 2005, 353, 704-718.

Saxena, A.M., Udgaonkar, J.B. & Krishnamoorthy, G.
Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with green fluorescent protein.
Protein Science, 2005, 14, 1787-1799.

Bhavesh, N.S., Juneja, J., Udgaonkar, J.B. & Hosur, R.V.
Native and non-native conformational preferences in the urea-unfolded state of barstar.
Protein Science, 2004, 13, 3085-3091,

Pradeep, L. & Udgaonkar, J.B.
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
J. Biol. Chem., 2004, 279, 40303-40313

Pradeep, L. & Udgaonkar, J.B.
Effect of salt on the urea-unfolded form of barstar probed by m value measurements.
Biochemistry, 2004, 43, 11393-11402,

Beena, K., Udgaonkar, J. B., and Varadarajan, R.
Effect of signal peptide on the stability and folding kinetics of maltose binding protein.
Biochemistry, 2004, 43, 3608-3619

Sridevi, K., Lakshmikanth, G., Krishnamoorthy, G. & Udgaonkar, J.B.
Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble.
J. Mol. Biol. (2004) .337, 699–711

Mallik, R., Udgaonkar, J.B. & Krishnamoorthy, G.
Kinetics of proton transfer in a green fluorescent protein: a laser-induced pH jump study.
Proc. Ind. Acad. Sci. (Chemical Sciences). 2003, 115(4); 307-317

Bhutani, N. & Udgaonkar, J.B.
Folding sub-domains of thioredoxin identified by native-state hydrogen exchange.
Protein Science, 2003, 12, 1719-1731

Rami, B.R., Krishnamoorthy, G. and Udgaonkar, J.B.
Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar.
Biochemistry, 2003, 42(26); 7986-8000

Sridevi, K. & Udgaonkar, J.B.
Surface expansion is independent of and occurs faster than core solvation during the unfolding of barstar.
Biochemistry, 2003 Feb.18; 42(6) 1551-1563

Pradeep, L and Udgaonkar, JB
Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar
Journal of Molecular Biology, 2002, 324, 331–347.

Juneja J, Bhavesh NS, Udgaonkar JB, Hosur RV.
NMR Identification and Characterization of the Flexible Regions in the 160 kD Molten Globule-Like Aggregate of Barstar at Low pH.
Biochemistry. 2002 Aug 6;41(31):9885-99.

Juneja J, Udgaonkar JB.
Characterization of the unfolding of ribonuclease a by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding.
Biochemistry. 2002 Feb 26;41(8):2641-54.

Rami BR, Udgaonkar JB.
Mechanism of formation of a productive molten globule form of barstar.
Biochemistry. 2002 Feb 12;41(6):1710-6.

Sridevi K, Udgaonkar JB.
Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates.
Biochemistry. 2002 Feb 5;41(5):1568-78.

Bhutani N, Udgaonkar JB.
GroEL channels the folding of thioredoxin along one kinetic route.
J Mol Biol. 2001 Dec 14;314(5):1167-79.

Rami BR, Udgaonkar JB.
pH-jump-induced folding and unfolding studies of barstar: evidence for multiple folding and unfolding pathways.
Biochemistry. 2001 Dec 18;40(50):15267-79.

Bhuyan AK, Udgaonkar JB.
Folding of horse cytochrome c in the reduced state.
J Mol Biol. 2001 Oct 5;312(5):1135-60.

Lakshmikanth GS, Sridevi K, Krishnamoorthy G, Udgaonkar JB.
Structure is lost incrementally during the unfolding of barstar.
Nat Struct Biol. 2001 Sep;8(9):799-804.

Ganesh C, Zaidi FN, Udgaonkar JB, Varadarajan R.
Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein.
Protein Sci. 2001 Aug;10(8):1635-44.

Sahu SC, Bhuyan AK, Udgaonkar JB, Hosur RV.
Backbone dynamics of free barnase and its complex with barstar determined by 15N NMR relaxation study.
J Biomol NMR. 2000 Oct;18(2):107-18.

Sahu SC, Bhuyan AK, Majumdar A, Udgaonkar JB.
Backbone dynamics of barstar: a (15)N NMR relaxation study.
Proteins: Structure Function and Genetics. 2000 Dec 1;41(4):460-74.

Sridevi K, Juneja J, Bhuyan AK, Krishnamoorthy G, Udgaonkar JB.
The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.
J Mol Biol. 2000 Sep 15;302(2):479-95.

Bhutani N, Udgaonkar JB.
A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar.
J Mol Biol. 2000 Apr 14;297(5):1037-44.

Ramachandran S, Rami BR, Udgaonkar JB.
Measurements of cysteine reactivity during protein unfolding suggest the presence of competing pathways.
J Mol Biol. 2000 Mar 31;297(3):733-45.

Venkatesha, B., Udgaonkar, J.B., Appaji Rao, N. & Savitri, H.S.
Guanidine hydrochloride-induced reversible unfolding of sheep liver serine hydroxymethyl transferase.
Journal of Bioscience, 1999, 24, 69-77.

Bhuyan AK, Udgaonkar JB.
Observation of multistate kinetics during the slow folding and unfolding of barstar.
Biochemistry. 1999 Jul 13;38(28):9158-68.

Panse VG, Udgaonkar JB, Varadarajan R.
SecB binds only to a late native-like intermediate in the folding pathway of barstar and not to the unfolded state.
Biochemistry. 1998 Oct 13;37(41):14477-83.

Bhuyan AK, Udgaonkar JB.
Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions.
Proteins. 1998 Aug 1;32(2):241-7.

Bhuyan AK, Udgaonkar JB.
Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state.
Biochemistry. 1998 Jun 23;37(25):9147-55.

Ratnaparkhi GS, Ramachandran S, Udgaonkar JB, Varadarajan R.
Discrepancies between the NMR and X-ray structures of uncomplexed barstar: analysis suggests that packing densities of protein structures determined by NMR are unreliable.
Biochemistry. 1998 May 12;37(19):6958-66.

Venkatesha B, Udgaonkar JB, Rao NA, Savithri HS.
Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase.
Biochim Biophys Acta. 1998 Apr 23;1384(1):141-52.

Bhuyan AK, Udgaonkar JB.
Two structural subdomains of barstar detected by rapid mixing NMR measurement of amide hydrogen exchange.
Proteins. 1998 Feb 15;30(3):295-308.

Zaidi FN, Nath U, Udgaonkar JB.
Multiple intermediates and transition states during protein unfolding.
Nat Struct Biol. 1997 Dec;4(12):1016-24.

Schoppe A, Hinz HJ, Agashe VR, Ramachandran S, Udgaonkar JB.
DSC studies of the conformational stability of barstar wild-type.
Protein Sci. 1997 Oct;6(10):2196-202.

Agashe VR, Schmid FX, Udgaonkar JB.
Thermodynamics of the complex protein unfolding reaction of barstar.
Biochemistry. 1997 Oct 7;36(40):12288-95.

Nath U, Udgaonkar JB.
Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway.
Biochemistry. 1997 Jul 15;36(28):8602-10.

Nath U, Agashe VR, Udgaonkar JB.
Initial loss of secondary structure in the unfolding of barstar.
Nat Struct Biol. 1996 Nov;3(11):920-3.

Swaminathan R, Nath U, Udgaonkar JB, Periasamy N, Krishnamoorthy G.
Motional dynamics of a buried tryptophan reveals the presence of partially structured forms during denaturation of barstar.
Biochemistry. 1996 Jul 16;35(28):9150-7.

Ramachandran S, Udgaonkar JB.
Stabilization of barstar by chemical modification of the buried cysteines.
Biochemistry. 1996 Jul 2;35(26):8776-85.

Agashe VR, Shastry MC, Udgaonkar JB.
Initial hydrophobic collapse in the folding of barstar.
Nature. 1995 Oct 26;377(6551):754-7.

Khurana R, Hate AT, Nath U, Udgaonkar JB.
pH dependence of the stability of barstar to chemical and thermal denaturation.
Protein Sci. 1995 Jun;4(6):1133-44.

Shastry MCR, Udgaonkar JB.
The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates.
J Mol Biol. 1995 Apr 14;247(5):1013-27.

Udgaonkar JB, Baldwin RL.
Nature of the early folding intermediate of ribonuclease A.
Biochemistry. 1995 Mar 28;34(12):4088-96.

Agashe VR, Udgaonkar JB.
Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride.
Biochemistry. 1995 Mar 14;34(10):3286-99.

Nath U, Udgaonkar JB.
Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate.
Biochemistry. 1995 Feb 7;34(5):1702-13.

Swaminathan, R., Periasamy, N., Udgaonkar, J.B. & Krishnamoorthy, G.
Molten globule-like conformation of barstar: a study by fluorescence dynamics.
J. Phys. Chem.1994, 98, 9270-9278.

Raghunathan V, Khurana S, Gupta V, Khurana R, Udgaonkar JB, Salunke DM.
Crystallization and molecular packing analysis of barstar crystals.
J Mol Biol. 1994 Oct 28;243(3):533-6.

Shastry MC, Agashe VR, Udgaonkar JB.
Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone.
Protein Sci. 1994 Sep;3(9):1409-17.

Khurana R, Udgaonkar JB.
Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule.
Biochemistry. 1994 Jan 11;33(1):106-15.

Udgaonkar JB, Baldwin RL.
Early folding intermediate of ribonuclease A.
Proc Natl Acad Sci U S A. 1990 Nov;87(21):8197-201.

Milburn T, Matsubara N, Billington AP, Udgaonkar JB, Walker JW, Carpenter BK, Webb WW, Marque J, Denk W, McCray JA, et al.
Synthesis, photochemistry, and biological activity of a caged photolabile acetylcholine receptor ligand.
Biochemistry. 1989 Jan 10;28(1):49-55.

Udgaonkar JB, Baldwin RL.
NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A.
Nature. 1988 Oct 20;335(6192):694-9.

Udgaonkar JB, Hess GP.
Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique.
Proc Natl Acad Sci U S A. 1987 Dec;84(24):8758-62.

Udgaonkar JB, Hess GP.
Acetylcholine receptor: channel-opening kinetics evaluated by rapid chemical kinetic and single-channel current measurements.
Biophys J. 1987 Nov;52(5):873-83.

Takeyasu K, Shiono S, Udgaonkar JB, Fujita N, Hess GP.
Acetylcholine receptor: characterization of the voltage-dependent regulatory (inhibitory) site for acetylcholine in membrane vesicles from Torpedo californica electroplax.
Biochemistry. 1986 Apr 8;25(7):1770-6.

Pasquale EB, Udgaonkar JB, Hess GP.
Single-channel current recordings of acetylcholine receptors in electroplax isolated from the Electrophorus electricus Main and Sachs' electric organs.
J Membr Biol. 1986;93(2):195-204.

Shiono S, Takeyasu K, Udgaonkar JB, Delcour AH, Fujita N, Hess GP.
Regulatory properties of acetylcholine receptor: evidence for two different inhibitory sites, one for acetylcholine and the other for a noncompetitive inhibitor of receptor function (procaine).
Biochemistry. 1984 Dec 18;23(26):6889-93.

Takeyasu K, Udgaonkar JB, Hess GP.
Acetylcholine receptor: evidence for a voltage-dependent regulatory site for acetylcholine. Chemical kinetic measurements in membrane vesicles using a voltage clamp.
Biochemistry. 1983 Dec 6;22(25):5973-8.

Pasquale EB, Takeyasu K, Udgaonkar JB, Cash DJ, Severski MC, Hess GP.
Acetylcholine receptor: evidence for a regulatory binding site in investigations of suberyldicholine-induced transmembrane ion flux in Electrophorus electricus membrane vesicles.
Biochemistry. 1983 Dec 6;22(25):5967-73.

Juneja, J. & Udgaonkar, J.B.
NMR studies of protein folding.
Current Science, 2003, 84, No. 2, 157-172

Bhutani N and Udgaonkar, JB
Chaperonins as protein folding machines.
Current Science, 2002, 83 1337-1351.

Udgaonkar, J.B.
Entropy in Biology.
Resonance, 2001, 6, 61-66.

Bhuyan, A.K. & Udgaonkar, J.B.
Real-time NMR measurements of protein folding and hydrogen exchange dynamics.
Current Science, 1999, 77, 942-950.

Nath, U. & Udgaonkar, J.B.
How do proteins fold?
Current Science, 72, 180-191.

Udgaonkar, J.B.
Folding in an unfolded protein
Current Science, 1993, 64, 7-9.

Udgaonkar, J.B. & Hess, G.P.
Acetylcholine receptor: isosteric properties
Trends in Pharm. Sci., 1987, 8, 190-192.

Hess GP, Udgaonkar JB, Olbricht WL.
Chemical kinetic measurements of transmembrane processes using rapid reaction techniques: acetylcholine receptor.
Annu Rev Biophys Biophys Chem. 1987;16:507-34. Review.

Udgaonkar JB, Hess GP.
Acetylcholine receptor kinetics: chemical kinetics.
J Membr Biol. 1986;93(2):93-109.

Saxena, A.M., Udgaonkar, J.B. & Krishnamoorthy, G.
Protein dynamics and protein folding dynamics revealed by time-resolved fluorescence.
Fluorescence Spectroscopy in Biology
(eds. Hof, M., Hutterer, R. & Fidler, V.) Springer, 2005,

Relevance of burst phase changes in optical signals of polypeptides during protein folding.
Perspectives in Structural Biology
(ed: Vijayan, M., Yathindra, N. & Kolaskar, A.S.), Universities Press, Hyderabad, 1999, 293-303.

Bhuyan, A.K. & Udgaonkar, J.B.
Multi-state kinetics of folding and unfolding of barstar.
Excerpta Medica International Congress Series (ICS), 24th Taniguchi International Symposium, Elsevier Science, 1999, 261-270.

Hess, G.P., Kolb, H.-A., Lauger, P., Schoffeniels, E., Schwartze, W., Udgaonkar, J.B. & Pasquale, E.B. in
Molecular Basis of Nerve Activity
(eds. Changeux, J.-P., Hucho, F. Maelicke, A. & Neumann, E.) 1985, pp. 317-334, Walter de Gruyter, New York.rajesh