Dr. Rajesh Kumar
Professor
Centre for Chemistry
School of Basic & Applied Sciences
Central University of Punjab
Bathinda- 151001
Email Id: rajesh.kumar@cup.edu.in; rajeshchem01@gmail.com
Mobile:

 

Education :

Degree/ Certificate	University /Institute	Year	Subject/ Specialization
Ph.D.	Hyderabad Central University, School of Chemistry	2006	Chemistry (Biophysical and Bioinorganic Chemistry
M.Phil.	Hyderabad Central University (2001), School of Chemistry	2001	Chemistry

Institute	Position	Period
Department of Chemistry, Central University of Punjab, Bathinda	Professor	2018 (December) - Current
Department of Chemistry, Central University of Punjab, Bathinda	Associate Professor	2015, Dec - 2018, Dec
School of Chemistry and Biochemistry, Thapar Institute of Engineering and Technology, Patiala,  Punjab, India.	Associate Professor	2014, July - 2015, Dec
School of Chemistry and Biochemistry, Thapar Institute of Engineering and Technology, Patiala,  Punjab, India	Assistant Professor	July 2006-Jun 2014
Canadian Blood Services/Canadian Institutes of Health Research, Centre for Blood Research and Department of Biochemistry and Molecular Biology, University of British Columbia, Canada  (Mentor Prof. Grant Mauk)	Postdoctoral Fellow	Jan 2007-Jan 2009
Hyderabad Central University, School of Chemistry	Research Fellow	Feb 2006 to July 2006

My research publications h-index of 12 and i10-index of 14 (Source: Google Scholar).

• Interactions of nanoparticles and ionic liquids with biomolecules.
• Advanced thermodymaic studies of biomolecules using isotermal and differrential scanning calorimeters (ITC and DSC)
• Advanced ultrafast protein folding study using laser flash photolysis and fluorescence correlation spectroscopy (FCS) in confogal microsopy in confocal microscopy.
• Structural and functional studies of metalloproteins using NMR, circular dichrosim (CD), steady state and time reolved fluorecence. and millisecond stopped mixing device  
• Mechanical unfolding study by single-molecule force spectroscopy

1. Head of Department (Jan 2016 to March 2020), Department of Chemistry, Central University of Punjab, Bathinda
2. Member, Executive Council (EC),  (Jun 2020 to till date) Central University of Punjab, Bathinda
3. Member, Academic Council (AC),  (Jun 2020 to till date), Central University of Punjab, Bathinda
4. Member, Internal Quality Assurance Cell (IQAC) ( July 2018 to Till Date), Central University of Punjab, Bathinda
5. Member School Board, School of Basic and Applied Sciences ( Jan 2016 to Till Date), Central University of Punjab, Bathinda
6.  Chairperson  (BOS, AAC, CDDC) (Jan 2016 to March 2020), Department of Chemistry, Central University of Punjab, Bathinda
7.  Member  (BOS, AAC, CDDC) (March 2020 to till date), Department of Chemistry, Central University of Punjab, Bathinda
8. Senate member:  (2015) Thapar Institute of Engineering and Technology, Patiala, 
9. SPPC Secretary (2015), School Planning & Policy Committee, School of Chemistry and Biochemistry, Thapar Institute of Engineering and Technology, Patiala

• Canadian Blood Services/Canadian Institutes of Health Research Personal Research Award in the Area of Transfusion Science (Jan 2007-2009)  
• DST Young Scientist Award
• NET Qualified in Chemical Sciences.
• DST/DBT-SRF
• BOS member, Dept. of Chemistry and Chemical Sciences, Central University of Jammu
• BOS member, Dept. of Chemistry, MRSPTU, Bathinda
• BOS member, Dept. of Chemistry, LPU, Phagwara,
• Reviewer for competitive grant programs (DST-SERB).
• External Expert (PhD and Master thesis, CSIR, JNU, AIMS-New Delhi, LPU, Thapar Institute , Patiala)
• Reviewer of several journals (Physical Chemistry B (ACS), Biochimica et Biophysica Acta (BBA-general subject), Protein Design, Engineering and Selection (PEDS), PLOS one, RSC advances, Analytical Method (RSC), etc), Photochemistry and Photobiology, Food & Function, Research in Microbiology, Journal of Functional Foods, Applied Biochemistry and Biotechnology, Engineering Reports, etc).

1. Prof. P. Guptasarma, Department of Biological Sciences, IISER, Mohali
2. Dr. Deepak Sharma, Senior Scientist, IMTECH, CSIR, Chandigarh
3. Prof. Abani K. Bhuyan, School of Chemistry, University of Hyderabad
4. Prof. Grant A Mauk, Department of Biochemistry and Molecular Biology, University of British Columbia, Canada
5. Dr. Vinay Kumar Yadav, Assistant Professor,  Dept. of Botany,  Central University of Punjab, Bathinda

1. Kumar, R. Kumar, D. Sharma, M. Garg, V. Kumar, and  M.C. Agarwal (2018) Macromolecular crowding-induced molten globule states of the alkali pH-denatured proteins, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol =1866, Pages=1102-1114 (Impact factor 2.54)
2. R. Kumar, D. Sharma, V. Kumar, R. Kumar (2018) Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro, Archives of Biochemistry and Biophysics, Vol =654, Pages=146-162 (Impact factor 3.56 ).
3. R. Jain, D. Sharma, R. Kumar and R. Kumar, (2019) Structural, kinetic and thermodynamic characterizations of SDS-induced molten globule state of a highly negatively charged cytochrome c, The Journal of Biochemistry, Vol= 125, Pages=125-137 (Impact factor= 2.476). 341-354.
   
4. M.Garg, B. Kumari and R.Kumar  (2019) Effect of 1-allyl-3-methylimidazoleum bromide on the motional dynamics and thermal stability of horse ferrocytochrome c Effect of 1-allyl-3-methylimidazoleum bromide on the motional dynamics and thermal stability of horse ferrocytochrome c. AIP Conference Proceedings 2142, 200002 (2019)
5. R. Jain, M. C. Agarwal, R. Kumar, D. Sharma,  and R. Kumar (2018)  Effects of lyotropic anions on thermodynamic stability and dynamics of horse cytochrome c, Biophysical Chemistry, Vol =240 Pages=88-97 (Impact factor= 2.0).
6. M. Muddassir, B. Manna, P. Singh, S. Singh, R. Kumar, A. Ghosh, D. Sharma (2018)  Single-molecule force-unfolding of titin I27 reveals a correlation between the size of the surrounding anions and its mechanical stability, Chemical Communications, Vol =54, Pages=9635-9638 (Impact factor= 6.164)
7. Kumar, S. Sharma, D., and Kumar, R. (2017) Role of Macromolecular Crowding on Stability and Iron Release Kinetics of Serum Transferrin. J Phys Chem B. ;121(37):8669-8683 (Impact factor 2.923).
8. Kumar, R. (2016) Analysis of the pH-dependent thermodynamic stability, local motions, microsecond folding kinetics of carbonmonoxycytochrome c. Archive of Biochemistry and Biophysics, 606, 16-25 (Impact factor 3.56).
9. Jain, R., Kumar, R., Kumar, S.,  Chhabra, R., Agarwal, M. , and Kumar, R. (2015) Analysis of the pH-Dependent Stability and Millisecond Folding Kinetics of Horse Cytochrome c. Archive of Biochemistry and Biophysics 585, 52-63 (Impact factor 3.56)
10. Kumar, R., Sharma, D., Jain, R., Kumar, S., and Kumar, R. (2015) Role of macromolecular crowding and salt ions on the structural-fluctuation of a highly compact configuration of carbonmonoxycytochrome c. Biophysical Chemistry 207, 61-73 (Impact factor= 2.0).
11. Rishu Jain, Deepak Sharma, Sandeep Kumar, Rajesh Kumar. Factor defining the effects of glycine betaine on the thermodynamic stability and internal dynamics of horse cytochrome c, Biochemistry (ACS), 53(32) (2014) 5221-5235 (Impact factor= 2.952).
12. Sandeep Kumar, Deepak Sharma, Rajesh Kumar, Rajesh Kumar. Electrostatic effects controls the stability and iron release kinetics of ovotransferrin, J. Biol. Inorg. Chem., 19(6) (2014) 1009-1024 (Impact factor= 3.632).
13. Sandeep Kumar, Deepak Sharma, Rajesh Kumar. Effect of urea and alkylureas on the stability and structural fluctuation of the M80-containing ω-loop of horse cytochrome c, mvt059 341-354 Biochimica et Biophysica Acta, 1844(3) (2014) 641–655 (Impact factor= 2.54).
14. Rishu Jain, Sandeep Kaur, Rajesh Kumar. Guanidine hydrochloride-induced alkali-molten globule model of horse ferrocytochrome c, Journal of Biochemistry, 153(2) (2013) 161-177 (Impact factor= 2.476). 341-354.  
15. Rishu Jain, Deepak Sharma, Rajesh Kumar. Effects of Alcohols on the Stability and Low-Frequency Local Motions that Control the Slow Changes in Structural Dynamics of Ferrocytochrome c, Journal of Biochemistry, 154 (4) mvt059 (2013) (Impact factor= 2.476). 341-354.
16. Rajesh Kumar, Rishu Jain, Rajesh Kumar. Viscosity-Dependent Structural Fluctuation of the M80-Containing Ω-Loop of Horse Ferrocytochrome c, Chemical Physics, 418 (2013) 57-64 (Impact factor= 1.771). 341-354..
17. Rajesh Kumar, A. Grant Mauk. Protonation and Anion Binding Control the Kinetics of Iron Release from Human Transferrin, J. Phys. Chem. B (ACS), 116(12) (2012) 3795-3807 (Impact factor 2.923).
18. Rajesh Kumar, A. Grant Mauk. Atypical Effects of Salts on the Stability and Irons Release Kinetics of Human Serum Transferrin, J. Phys. Chem. B., 113(36) (2009) 12400-12409 (Impact factor 2.923).
19. Rajesh Kumar, A. Grant Mauk. Iron Release from Human Transferrin in the Absence of Chelators Involves Five Kinetic Steps at Acidic pH, J. Biol. Inorg. Chem.14, (2009) S185-S224 (Impact factor= 3.632).
20. Rajesh Kumar, Abani K. Bhuyan. Entropic Stabilization of Myoglobin by Subdenaturing Concentrations of Guanidine Hydrochloride, J. Biol. Inorg. Chem., 14(1) (2009) 11-21 (Impact factor= 3.632).
21. Rajesh Kumar, Abani K. Bhuyan. Viscosity Scaling for the Glassy Phase of Protein Folding, J. Phys. Chem. B 112(39) (2008) 12549-12554 (Impact factor 2.923).
22. M. Yadaiah, Rajesh Kumar, Abani K. Bhuyan. Glassy dynamics in the folding landscape of cytochrome c: Detected by laser photolysis”, Biochemistry (ACS), 46(9) (2007) 2545-2551 (Impact factor= 2.952).
23. Rajesh Kumar, Abani K. Bhuyan. Effect of guanidine hydrochloride on stability and dynamics of myoglobin, J. Biol. Inorg. Chem., 112 (2007) S223-S230 (Impact factor= 3.632).
24. Rajesh Kumar, N. Prakash Prabhu, D. Krishna Rao, Abani K. Bhuyan, The Alkali Molten Globule State of Horse Fericytochonne c: Observation of Cold Denaturation, J. Mol. Biol., 364(3) (2006) 483-495 (Impact factor= 5.067).
25. Krishna Rao, Rajesh Kumar, M. Yadaiah, Abani K. Bhuyan. The Alkali Molten Globule State of Ferrocytochrome c: Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics, Biochemistry (ACS), 45(10), (2006) 3412-3420 (Impact factor= 2.952).
26. Rajesh Kumar, N. Prakash Prabhu, Abani K. Bhuyan. Ultrafast Events in the Folding of Ferrocytochrome c, Biochemistry (ACS), 44 (26) (2005) 9359-9367 (Impact factor= 2.952).
27. Rajesh Kumar, Abani K. Bhuyan. Two-state Folding of Horse Ferrocytochrome c: Analyses of Linear Free Energy Relationship, Chevron Curvature, and Stopped-Flow Burst Relaxation Kinetics, Biochemistry (ACS), 44(8) (2005) 3024-3033 (Impact factor= 2.952).
28. N. Prakash Prabhu, Rajesh Kumar, Abani K. Bhuyan. Folding barrier in horse cytochrome c: Support for a classical folding pathway, J. Mol. Biol., 337(1) (2004) 195-208  (Impact factor= 5.067).
29. Rajesh Kumar, N. Prakash Prabhu, M. Yadaiah, Abani K. Bhuyan. Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride, Biophysical J., 87(4) (2004) 2656- 2662 (Impact factor= 3.854).
30. Abani K. Bhuyan, Rajesh Kumar (2002) Kinetic barriers to the folding of horse cytochrome c in the reduced state, Biochemistry (ACS), 41(42) (2002) 12821-12834 (Impact factor= 2.952).

S. No.	Title	Agency	Period	Grant
1.	Kinetic and Thermodynamic Studies of the Effects of Synergistic and Nonsynergistic Anions on Blood Plasma Transferrin.	SERB-DST Govt. of INDIA	2015-2018.	Rs.-52.63 lacs
2.	The Mechanism of Reductive Release of Iron from Serum Transferrin,	ICMR, Govt. Of INDIA	2015-2018	Rs.-39.12 lacs
3.	The Role of Macromolecular Crowding on Structure, Function, Stability and Folding of Serum Transferrin.	DBT Govt. Of INDIA	2016-2018.	Rs.-24.72 lakhs
4.	Structural, Kinetic and Thermodynamic Studies on Macromolecular Crowding on Eye Lens Crystallins	CUPB (Internally funded)	2017-2019	Rs.-3.0 lakhs
5.	The Kinetics and Mechanism of Iron Release from Transferrins: Rs.-18.5 lakhs sanctioned by DST (DST-Young Scientist Scheme).	DST, Govt. of INDIA	(2010-2013)	Rs.-18.2 lacs
6.	Ki   Kinetic and Thermodynamics Studies on the Effect of Chaotropic and Kosmotropic Coslovents on Horse Ferrocytochrome c,	CSIR, Govt. of INDIA	2011-2014	Rs. 21.2 lacs
7.	pH-dependent stability and microsecond-folding kinetics of    horse ferrocytochrome c	UGC, Govt. of INDIA	2013-2015	Rs. 11.5 lacs
8.	The Mechanism of Iron Release from Transferrins	Research grant- in-aid scheme, Thapar University, Patiala	2009-2010	Rs. 1.0 lakh

Research Collaborators :

List of PhD Thesis Supervised (03):

List of PhD Thesis and JRF-CSIR Ongoing:

M.Sc. Students: Master Thesis Supervised = 25 students

Sl. No.	Topic/Title of Lecture/Paper	Title of Conference/ Seminar	Organized by & Date	International (Abroad or within country) / National
1	Role of Macromolecular Crowding on Structural, Kinetic and Thermodynamic Properties of Metalloproteins (invited talk).	Annual Symposium of the Indian Biophysical Society, 22-25 March 2017, IISER Mohali, Punjab	Indian Biophysical Society, IISER Mohali, Punjab	National
2	Guanidine Hydrochloride-Induced Folding and Stabilization of Alkali-Denatured Carbonmonoxycytochrome c. (paper presented)	International Symposium on Protein Folding and Dynamics	NCBS, Bangalore.	International (within country)
3	Thermodynamic Analysis of Effect of Alcohols on  Thermal Stability of Horse  Ferrocytochrome c. (paper presented)	International Symposium on Protein Folding and Dynamics	NCBS, Bangalore.	International (within country)
4	Iron Release from Diferric Ovotransferrin in the Absence of Chelators Involves Six Kinetic Steps at Acidic pH, (paper presented)	6th National Conference on Thermodyna​mics of Chemical and Biological Systems,	Department of   Chemistry, Maharshi Dayanand University, Rohtak,	National
5	Effect of neutral salts on the stability of acid denatured hen egg white lysozyme . (paper presented)	Material Research Society of India (23rd Annual meeting,.	Thapar University	National
6	Atypical effect of salts on the stability of  Fe3+-ovotransferrin CO32- complex. (paper presented)	Material Research Society of India, 23rd Annual meeting,	Thapar University	National
7	Entropic stabilization of Ferrocytochrome c by subdenaturing concentrations of methanol. (paper presented)	Material Research Society of India, 23rd Annual meeting,	Thapar University	National
8	Effect of neutral salts on the stability and dynamics of horse cytochrome c. (paper presented)	National Conference on Emerging Trends in Chemistry Biology Interface,)	Kumaun University, Nainital.	National
9	The size of anions and crowding agents control the local dynamics of a native-like compact state of horse ferrocytochrome c (paper presented)	NCIMSF 2013	Thapar University, Patiala	National
10	Hydrophobicity of denaturants control the local dynamics of a native-like compact state of horse ferrocytochrome c (paper presented)	NCIMSF 2013	Thapar University, Patiala	National
11	The glycine effect on release of iron from transferrins (paper presented)	NCIMSF 2013	Thapar University, Patiala	National
12	The Mechanism of Iron Release From Human Transferrin (paper presented)	National Symposium on Green Chemistry	Thapar University, Patiala	National
13	Analysis of the pH-Dependent Thermodynamic Stability, Local Motions, and Microsecond Folding Kinetics of Carbonmonoxycytochrome c (paper presented)	2nd Conference on Microscopy in Materials Science (AMST-2016)	School of Physics and Materials Science, Thapar University and Academy of Microscope Science and Technology.	National
14	Kinetic and Mechanism of Iron Release from Blood Plasma Transferrin (Invited talk)	2nd Conference on Microscopy in Materials Science (AMST-2016)	School of Physics and Materials Science, Thapar University and Academy of Microscope Science and Technology.	National
15	Effect of 1-Allyl-3-Methylimidazolium Bromide on the Motional Dynamics and Thermal Stability of Horse Ferrocytochromec (accepted)	International conference on advances in basic sciences (ICBAS-19)	GDC Memorial College  Bahal-1, 7-9 Feb 2019	International (within country)
16	Effects of Osmolytes on the Stability and Motional Dynamics of Horse Ferrocytochrome c	National Conferences on Advances in Chemical Engineering, (Editors P.K. Bajpai and H. Bhunia, Macmillan Advanced Research Series)	Thapar, University, Patiala, Feb27-28, 2011	National
19	Chairing session	National Conferences on Advances in Chemical Engineering, (Editors P.K. Bajpai and H. Bhunia, Macmillan Advanced Research Series)	Thapar, University, Patiala, Feb27-28, 2011	National
20	Thermodynamic, Structural and Functional Studies of MetalloproKineticteins (Invited talk)	National Conference on “Emerging Scenario in Basic & Applied Sciences for Sustainable Development,	DAV College Bathinda, 5th April 2018	National

Physical Principles of Structure, Function, and Motions of Biological Molecules: In order to confront the enigmatic issues of structure, folding, energy, motion, and function of several proteins and enzymes (cytochrome c, myoglobin, lyozymes, titin I27, transferrins), my research work interfaces physics, chemistry, and biology using advanced ultrafast kinetic (millisecond stopped flow, nanosecond laser flash photolysis), spectroscopic (NMR, UV-visible, fluorescence, Circular Diochroism (CD), double derivative FTIR etc), thermodynamic (differential scanning and isothermal calorimetery (DSC and ITC)), and single molecule atomic force clam spectroscopic techniques (SMFCS). Basic calculations in conjunction with kinetic, mechanical and structural modeling facilitate interpretation of the results (Archives of Biochemistry and Biophysics (2018), 654, 146-162, Chemical Communications (2018), 54, 9635-9638, Biochemistry (ACS), 53(32) (2014) 5221-5235). 

Iron Metabolism and Transport Proteins: Blood plasma serum transferrin (Tf) is the principal protein involved in iron metabolism that we are studying. Tf is primarily responsible for transport and distribution of iron from the gut and liver to tissues requiring iron. For this protein, our general approach is to apply a variety of spectroscopic (UV-visible, fluorescence, Circular Dichroism (CD), FTIR), fast kinetic (millisecond stopped flow), thermodynamic (ITC and DSC), and mechanistic (single molecule atomic force clam spectroscopy) techniques to characterize the manner in which the protein environment influences the chemical and physical properties of the iron center. (J Phys Chem B (ACS) (2017) ;121(37):8669-8683); J. Phys. Chem. B (ACS), 116(12) (2012) 3795-3807, J. Phys. Chem. B (ACS)., 113(36) (2009) 12400-12409.

Sr. No.	Name of the Equipment	Model and Make, Age of Equipment	Equipment available with
1.	CD Spectrometer MOS-500	Biologic France, 2years	With group
2.	Millisecond stopped flow MOS/200 M and With MOS 500	Biologic France, 2years	With group
3.	Fast Protein Liquid Chromatography	GE-Health, 2 years	With group
4.	Differential Scanning Calorimeter	Microcal-Peak-DSC	Department
5.	Isothermal  Calorimeter	Microcal-Peak-ITC	Department
6.	UV-VIS Spectrophotometer with palter	Shimadzu, Japan,	Department
7.	Litesizer DLS Particle Size Analyzer	Anta par, ordered	Department
8.	FTIR spectrophotometers	Bruker, six years	University central Facility
9.	NMR (600 MHz)	JEOL	University central Facility
10.	Confocal Laser Scanning Microscope with Florescence Correlation Spectroscopy	Olympus, Japan. Four years	University central Facility
11.	Fluorescence Microscope	Olympus, Japan. Four years	University central Facility
12.	XRD	Bruker	University Central Facility
13.	FESEM	Carl Zeiss, Germany, 4 years	University Central Facility
14.	DNA Sequencer	Applied Biosystems, 7 years	University Central Facility
15.	Atomic Absorption Spectorphotomer	Shimadzu, Japan 6years	University Central Facility
16.	ICP-MS	Shimadzu, Japan 2years	University Central Facility
17.	Ultra pure water purification system	1.5 year	University Central Facility
18.	Flow Cytometer	BD Diagnostics USA, 3 years	University Central Facility
19.	Refrigerator (-10 °C)	LG, INDIA	With PI's
20.	UPLC	hermo Scientific, 6 years	University Central Facility
21.	pH meter	3 years	With PI
22.	Laminar flow	2 Years	PI's Department
23.	Weighing balances to the accuracy of 4 and 5 digits after the decimal	2 Years	With PI, department
24.	GC-MS	Shimadzu Japan	University Central Facility
25.	Bioanalyzer	ERBA USA, 4 years	University Central Facility