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अखिल भारतीय आयुर्विज्ञान संस्थान, नई दिल्ली
All India Institute Of Medical Sciences, New Delhi
कॉल सेंटर:  011-26589142

M.Sc. Biophysics Syllabus

M.Sc. Biophysics Syllabus

PAPER I

Cell biology: Organization and structure of prokaryotes and eukaryotes, nucleus, cytoplasm, plasma membrane, mitochondria-structure, function respiratory chain and ATP synthesis, endoplasmic reticulum, golgi apparatus, membranes, ribosomes, peroxisomes, lysozomes, transcription and translation, transport of proteins, cancer and its molecular genetics, oncogenes, tumor suppression gene

Molecular biology: central dogma, genetic code, gene and operon, structure of DNA and RNA, plasmids, selectable markers, agarose gel, PCR, cloning PCR products, expression vectors, cell free translation, c- DNA libraries, genomic libraries, DNA micro arrays, DNA sequencing

Bioinformatics: Introduction, repositories, databases, pairwise sequence based alignment, relationship between sequence and structures, structural bioinformatics, genomics, proteomics, human genome project, software packages

Numerical methods: Introduction to numerical methods, solutions to non-linear algebraic equations by the method of iteration and Newton aphson method, numerical integration by trapezoidal rule and simpson’s rule, numerical solution of ordinary differential equations by picard’s method of successive approximation, Euler’s method and Runge-Kutta method

Dynamics of non-linear processes: Physico-mathematical foundations of the dynamics of non-linear processes, phase plane method, different modes of excitations, nearly sinusoidal oscillations, building up of oscillations, effect of third harmonic distortion, Liapounov criteria of stability, limit cycles

PAPER II

Elementary crystallography: Introduction, symmetry in crystals, lattices and unit cells, crystal systems, Bravais lattices, elements of symmetry- rotation axis, mirror planes and center of inversion, point group symmetry- monoaxial point groups, polyaxial point groups, translational symmetry- screw axis and glide planes, space group, equivalent points, X-ray diffraction and Bragg equation 

X-ray diffraction methods: scattering factor, structure factor expression, reciprocal lattice, Ewald’s sphere, electron density equation, phase problem, Patterson function, molecular replacement method, isomorphous replacement, refinement programs and interpretation of results, methods of data collection of crystal containing small molecule and large molecule, factors affecting the measurement of integrated intensities, photographic methods, diffractometers, area detectors and image plates.

Proteins : Purification, structure and function: twenty amino acids: structure and function, the peptide bond, primary structure of a protein: methods of sequence determination, forces determining protein structure, secondary structure of a protein: β strands, β sheets (parallel and anti parallel), β turns, α helix, 3.10 helix and π helix (differences), tertiary structure of a protein: protein folds-all alpha helix motifs (Lone helix, helix-turn-helix, four helix bundle and eight helix bundle), protein folds-all β sheet motifs (β sandwich, β barrel, greek Key topology and β propellars), protein folds- α / β motifs (Tim barrel, Rosman fold, α/β horseshoe), quaternary structure of a protein: macromolecular assemblies, domains and domain swapping, membrane proteins, purification methods, studies of proteins with MALDI-TOF, enzymes and enzyme kinetics, G-proteins and G-protein coupled receptors(GPCRs), proteins as targets for rational structure based drug design

Principles of nucleic acid structure: nucleotide structure and properties: Introduction to DNA, RNA, bases, sugars, phosphates, structure of nucleotide, nucleosides and polynucleotides and their nomenclature scheme. tautomerisation and ionization. genetic code. stereochemistry: nucleoside, torsion angles, sugar confirmation, NMR study, DNA structure: different types of DNA and their structure, DNA motifs, DNA repeats and their significance, function and stability, spectroscpic study of DNA: dye binding, interaction, denaturation, and renaturation of DNA, thermal denaturation and Tm value, RNA: structure and properties, different forms of RNA and their significance, alkaline hydrolysis of RNA, how it differs from DNA, role of 2’OH group, structure of phenylalanine tRNA, enzymes involved in molecular biology: DNA polymerase, RNA polymerase, reverse transcriptase, restriction endonuclease. DNA interaction: protein, dye, drugs and carcinogens, DNA replication: DNA polymerization, mutation, and DNA repair, DNA transcription: RNA synthesis, types of RNA polymerase, DNA polymorphism: repeats of DNA and their significance, single nucleotide polymorphism, c-DNA, cloning and expression and purification

Membrane Biology: Lipid structure and their organization, comparison of different membrane models, diffusion and permeability, different types of transport systems across membranes, liposome and its applications

Peptides-design, synthesis and applications: Introduction to peptides, peptide design, synthesis of peptides (solution phase and solid phase), protection and deprotection of amino and carboxyl group, unnatural amino acids, conformation of peptides, purification and crystallization of peptides, determination of structure of small molecules (briefly), application of peptides

PAPER III

Mathematical methods and their applications in biological systems: Ordinary differential equations of the first degree and first order (variable separable method, linear equation), linear differential equations of the second order with constant coefficients, the Laplace Transform, Inverse Laplace transform, application of Laplace transform to solutions of differential equations, Fourier series and their applications.

Quantum biology and its uses: Classical mechanics, Newton, Lagrange and Hamilton’s equations, Schrodinger’s equation and its complete solution for S.H.O, central force and angular momentum

Quantum chemistry: Atomic orbital models, the wave equation, molecular orbitals, the LCAO method, the overlap method, coulomb and resonance integrals, the hydrogen molecule, charge distributions, approximate methods.

Theoretical modeling of biomolecular systems: Basic principles of modeling, modeling by energy minimization technique, concept of rotation about bonds, energy minimization by basic technique for small molecules, Ramachandran plot, torsional space minimization, energy minimization in cartesian space, molecular mechanics-basic principle, molecular dynamics basic principles

Spectroscopic techniques: Introduction to spectroscopy, basic principles, instrumentation and applications of UV-VIS absorption, infrared, Raman, atomic absorption, fluorescence, circular dichroism, Laser spectroscopy, nuclear magnetic resonance, electron spin resonance, acoustic spectroscopy; solvent perturbation; difference spectroscopy; Fourier transform techniques; applications of Laser; mass spectroscopy.

 

         

 

 

M.Sc. Biophysics Syllabus

PAPER I

Cell biology: Organization and structure of prokaryotes and eukaryotes, nucleus, cytoplasm, plasma membrane, mitochondria-structure, function respiratory chain and ATP synthesis, endoplasmic reticulum, golgi apparatus, membranes, ribosomes, peroxisomes, lysozomes, transcription and translation, transport of proteins, cancer and its molecular genetics, oncogenes, tumor suppression gene

Molecular biology: central dogma, genetic code, gene and operon, structure of DNA and RNA, plasmids, selectable markers, agarose gel, PCR, cloning PCR products, expression vectors, cell free translation, c- DNA libraries, genomic libraries, DNA micro arrays, DNA sequencing

Bioinformatics: Introduction, repositories, databases, pairwise sequence based alignment, relationship between sequence and structures, structural bioinformatics, genomics, proteomics, human genome project, software packages

Numerical methods: Introduction to numerical methods, solutions to non-linear algebraic equations by the method of iteration and Newton aphson method, numerical integration by trapezoidal rule and simpson’s rule, numerical solution of ordinary differential equations by picard’s method of successive approximation, Euler’s method and Runge-Kutta method

Dynamics of non-linear processes: Physico-mathematical foundations of the dynamics of non-linear processes, phase plane method, different modes of excitations, nearly sinusoidal oscillations, building up of oscillations, effect of third harmonic distortion, Liapounov criteria of stability, limit cycles

PAPER II

Elementary crystallography: Introduction, symmetry in crystals, lattices and unit cells, crystal systems, Bravais lattices, elements of symmetry- rotation axis, mirror planes and center of inversion, point group symmetry- monoaxial point groups, polyaxial point groups, translational symmetry- screw axis and glide planes, space group, equivalent points, X-ray diffraction and Bragg equation 

X-ray diffraction methods: scattering factor, structure factor expression, reciprocal lattice, Ewald’s sphere, electron density equation, phase problem, Patterson function, molecular replacement method, isomorphous replacement, refinement programs and interpretation of results, methods of data collection of crystal containing small molecule and large molecule, factors affecting the measurement of integrated intensities, photographic methods, diffractometers, area detectors and image plates.

Proteins : Purification, structure and function: twenty amino acids: structure and function, the peptide bond, primary structure of a protein: methods of sequence determination, forces determining protein structure, secondary structure of a protein: β strands, β sheets (parallel and anti parallel), β turns, α helix, 3.10 helix and π helix (differences), tertiary structure of a protein: protein folds-all alpha helix motifs (Lone helix, helix-turn-helix, four helix bundle and eight helix bundle), protein folds-all β sheet motifs (β sandwich, β barrel, greek Key topology and β propellars), protein folds- α / β motifs (Tim barrel, Rosman fold, α/β horseshoe), quaternary structure of a protein: macromolecular assemblies, domains and domain swapping, membrane proteins, purification methods, studies of proteins with MALDI-TOF, enzymes and enzyme kinetics, G-proteins and G-protein coupled receptors(GPCRs), proteins as targets for rational structure based drug design

Principles of nucleic acid structure: nucleotide structure and properties: Introduction to DNA, RNA, bases, sugars, phosphates, structure of nucleotide, nucleosides and polynucleotides and their nomenclature scheme. tautomerisation and ionization. genetic code. stereochemistry: nucleoside, torsion angles, sugar confirmation, NMR study, DNA structure: different types of DNA and their structure, DNA motifs, DNA repeats and their significance, function and stability, spectroscpic study of DNA: dye binding, interaction, denaturation, and renaturation of DNA, thermal denaturation and Tm value, RNA: structure and properties, different forms of RNA and their significance, alkaline hydrolysis of RNA, how it differs from DNA, role of 2’OH group, structure of phenylalanine tRNA, enzymes involved in molecular biology: DNA polymerase, RNA polymerase, reverse transcriptase, restriction endonuclease. DNA interaction: protein, dye, drugs and carcinogens, DNA replication: DNA polymerization, mutation, and DNA repair, DNA transcription: RNA synthesis, types of RNA polymerase, DNA polymorphism: repeats of DNA and their significance, single nucleotide polymorphism, c-DNA, cloning and expression and purification

Membrane Biology: Lipid structure and their organization, comparison of different membrane models, diffusion and permeability, different types of transport systems across membranes, liposome and its applications

Peptides-design, synthesis and applications: Introduction to peptides, peptide design, synthesis of peptides (solution phase and solid phase), protection and deprotection of amino and carboxyl group, unnatural amino acids, conformation of peptides, purification and crystallization of peptides, determination of structure of small molecules (briefly), application of peptides

PAPER III

Mathematical methods and their applications in biological systems: Ordinary differential equations of the first degree and first order (variable separable method, linear equation), linear differential equations of the second order with constant coefficients, the Laplace Transform, Inverse Laplace transform, application of Laplace transform to solutions of differential equations, Fourier series and their applications.

Quantum biology and its uses: Classical mechanics, Newton, Lagrange and Hamilton’s equations, Schrodinger’s equation and its complete solution for S.H.O, central force and angular momentum

Quantum chemistry: Atomic orbital models, the wave equation, molecular orbitals, the LCAO method, the overlap method, coulomb and resonance integrals, the hydrogen molecule, charge distributions, approximate methods.

Theoretical modeling of biomolecular systems: Basic principles of modeling, modeling by energy minimization technique, concept of rotation about bonds, energy minimization by basic technique for small molecules, Ramachandran plot, torsional space minimization, energy minimization in cartesian space, molecular mechanics-basic principle, molecular dynamics basic principles

Spectroscopic techniques: Introduction to spectroscopy, basic principles, instrumentation and applications of UV-VIS absorption, infrared, Raman, atomic absorption, fluorescence, circular dichroism, Laser spectroscopy, nuclear magnetic resonance, electron spin resonance, acoustic spectroscopy; solvent perturbation; difference spectroscopy; Fourier transform techniques; applications of Laser; mass spectroscopy.

 

         

 

 

M.D Biophysics Syllabus

M.D Biophysics Syllabus

PAPER I

Molecular Pharmacology: definition and determination of important pharmaco-kinetic parameters and pharmaco-dynamic parameters, pharmacokinetic basis of individual difference in response to drugs, pharmacokinetic properties, pharmacopore identification, influence of structural modifications on pharmacokinetic properties, mode of action of drugs, quantitative structure activity relationship, present and future aids to drug design, structure and confirmation of drugs and receptors, drug receptor binding forces, structural aspects of drug-nucleic acid interactions

Peptides-design, synthesis and applications: introduction to peptides, peptide design, synthesis of peptides (solution phase and solid phase), protection and deprotection of amino and carboxyl group, unnatural amino acids, conformation of peptides, purification and crystallization of peptides, determination of structure of small molecules (briefly), application of peptides

Biomechanics: Basic concepts of fluid dynamics, Bernoulli equation and its applications, streamline flow, Reynolds number, viscous flow, effects of gravity and external acceleration on circulation

Biostatistics: mean, median, mode, dispersion, standard deviation, correlation and regression, T-Test, chi-square test, F-test, ANOVA, how to enter data, edit and transform data, descriptive statistics ie. how to calculate mean, SD, range etc., frequency distribution, hypothesis tests for means and proportions, ANOVA, scatter plot, correlation matrix, regression, probability distribution.

Bioinformatics: Introduction, repositories, databases, pairwise sequence based alignment, relationship between sequence and structures, structural bioinformatics, genomics, proteomics, human genome project, software packages

Clinical proteomics

 

PAPER II

Spectroscopic techniques: Introduction to spectroscopy, basic principles, instrumentation and applications of UV-VIS absorption, infrared, Raman, atomic absorption, fluorescence, Circular dichroism, Laser spectroscopy, nuclear magnetic resonance, electron spin resonance, acoustic spectroscopy; solvent perturbation; difference spectroscopy; Fourier transform techniques; applications of Laser; mass spectroscopy.

Elementary crystallography: Introduction to crystallography, symmetry in crystals, lattices and unit cells, crystal systems, Bravais lattices, elements of symmetry- rotation axis, mirror planes and center of inversion, point group symmetry- monoaxial point groups, polyaxial point groups, translational symmetry- screw axis and glide planes, space group, equivalent points, X-ray diffraction and Bragg’s equation

X-ray diffraction methods: Scattering factor, structure factor expression, reciprocal lattice, Ewald’s sphere, electron density equation, phase problem, Patterson function, molecular replacement method, isomorphous replacement, refinement programs and interpretation of results, methods of data collection of crystal containing small molecule and large molecule, factors affecting the measurement of integrated intensities, photographic methods, diffractometers, area detectors and image plates.

Separation techniques: Basic principles and applications of electrophoresis-types of electrophoresis, estimation of molecular weight of proteins by logirthmic method; basic principles and applications of centrifugation-sedimentation, estimation of sedimentation rate by sedimentation velocity method and equilibrium method; basic principles and applications of chromatography-capacity factor of the gel, Kd value, α value.

Molecular modeling: Basic principle of modeling, modeling by energy minimization technique, concept of rotation about bonds, energy minimization by basic technique for small molecules, Ramachandran plot, torsional space minimization, energy minimization in cartesian space, molecular mechanics-basic principle, molecular dynamics basic principles

 

PAPER III

Cell biology: Organization and structure of prokaryotes and eukaryotes, nucleus, cytoplasm, plasma membrane, mitochondria-structure, function respiratory chain and ATP synthesis, endoplasmic reticulum, golgi apparatus, membranes, ribosomes, peroxisomes, lysozomes, transcription and translation, transport of proteins, cancer and its molecular genetics, oncogenes, tumor suppression gene

Molecular biology: central dogma, genetic code, gene and operon, structure of DNA and RNA, plasmids, selectable markers, agarose gel, PCR, Cloning PCR products, expression vectors, cell free translation, c- DNA libraries, genomic libraries, DNA micro arrays, DNA sequencing

Proteins, purification, structure and function: twenty amino acids: structure and function, the peptide bond, primary structure of a protein: methods of sequence determination, forces determining protein structure, secondary structure of a protein: β strands, β sheets (parallel and anti parallel), β turns, α helix, 310 helix and π helix (differences), tertiary structure of a protein: protein folds-all α helix motifs (Lone helix, helix-turn-helix, four helix bundle and eight helix bundle), protein folds-all β sheet motifs (β sandwich, β barrel, greek Key topology and β propellars), protein folds- α / β motifs (Tim barrel, Rosman fold, α/β horseshoe), quaternary structure of a protein: macromolecular assemblies, domains and domain swapping, membrane proteins, purification methods, studies of proteins with MALDI-TOF, enzymes and enzyme kinetics, G-proteins and G-protein coupled receptors(GPCRs), proteins as targets for rational structure based drug design

Principles of nucleic acid structure: nucleotide structure and properties: introduction to DNA, RNA, bases, sugars, phosphates, structure of nucleotide, nucleosides and polynucleotides and their nomenclature scheme. tautomerisation and ionization. genetic code. stereochemistry: nucleoside, torsion angles, sugar conformation, NMR study, DNA structure: different types of DNA and their structure, DNA motifs, DNA repeats and their significance, function and stability, spectroscpic study of DNA: dye binding, interaction, denaturation, and renaturation of DNA, thermal denaturation and Tm value, RNA: structure and properties, different forms of RNA and their significance, alkaline hydrolysis of RNA, how it differs from DNA, role of 2’OH group, structure of phenylalanine tRNA, enzymes involved in molecular biology: DNA polymerase, RNA polymerase, reverse transcriptase, restriction endonuclease. DNA interaction: protein, dye, drugs and carcinogens, DNA replication: DNA polymerization, mutation, and DNA repair, DNA transcription: RNA synthesis, types of RNA polymerase, DNA polymorphism: repeats of DNA and their significance, single nucleotide polymorphism, c-DNA, cloning and expression and purification

Membrane biology: Lipid structure and their organization, comparison of different membrane models, diffusions and permeability, different types of transport system across membranes, liposome and its applications

 

PAPER IV

Imaging techniques: Ultrasound, nuclear magnetic resonance, positron emission topography, computer axial tomography, whole body scanner, dose calibrators, gamma scintillation camera, digital imaging techniques, acquisition, analysis and processing of data from gamma camera, enhancement, topographic reconstruction, display and recording of image

Radiation biophysics: production and types of radiations, radiation measurement units, interaction of radiation with matter, detection of radiation by ionization chamber, G.M counter, proportional counter, liquid scintillation counter, radiation protection, molecular effects of radiation on membranes, cytoplasmic organelles, macromolecules, factors modifying effects of radiation, repairs of radiation induced damage

Radio pharmaceuticals: Production of radionuclides by reactors, cyclotrons and particle accelerators, use of radionuclide generators, elements of radiochemistry

Diagnostic use of radionuclides: In vivo imaging and functional studiesof brain, thyroid, heart, biliary tract, liver, kidney, spleen, tumors, bones and abscesses, use of imaging devices and external detectors for organ imaging, time dependent and differential functional studies, use of physiological gating techniques for functional studies, methodology and quality control of competitive binding and radio immunoassay, procedures for the measurement of peptide hormones, drugs and other biological substances, basic principles of radionuclide therapy in thyrotoxicosis and carcinoma thyroid

Bioelectric potentials: Principles and interpretations of electro-encephalogram, electro-cardiogram and electro-retionogram

Dynamics of non-linear Processes: Physico-mathematical foundations of the dynamics of non-linear processes, phase plane method, different modes of excitations, nearly sinusoidal oscillations, building up of oscillations, effect of third harmonic distortion, Liapounov criteria of stability, limit cycles

 

         

 

 

 

Prof. Savita Yadav

Prof. Savita Yadav

 
Designation Professor
Email यह ईमेल पता spambots से संरक्षित किया जा रहा है. आप जावास्क्रिप्ट यह देखने के सक्षम होना चाहिए.  ;  यह ईमेल पता spambots से संरक्षित किया जा रहा है. आप जावास्क्रिप्ट यह देखने के सक्षम होना चाहिए.
Contact Number +91-11-26594608 ; +91-11-26593201
Research Interests

 

Protein Science and Functional Biophysics to gain molecular insights of mechanisms of medically relevant biological processes related to male infertility, prostate cancer, oral carcinomas and dental caries ; Clinical and expression proteomics for identifying disease biomarkers ; Proteomics of medicinal plants for screening clinically relevant proteins.
Awards and Honors
AIIMS Excellence Award (2013)
Member, National Academy of Medical Sciences
Best Poster Presentation Award’ from Indian Science Congress Association (2003). 
Young scientist Award’ from Indian Science Congress Association (1991).
Life member of Proteomics Society of India, Indian Biophysical Society, Indian Science Congress  Association, Indian Crystallographic Association, Human Proteome Organization
Remained Nominated member of Bureau of Legislative Assembly of Delhi Legislative Assembly.
Recent Significant Publications

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Kumar S, Tomar AK, Singh S, Gill K, Dey S, Singh S, Yadav S.Heparin binding carboxypeptidase E protein exhibits antibacterial activity in human semen. Int J Biol Macromol. 2014 Mar;64:319-27.
Binita K, Kumar S, Sharma VK, Sharma V, Yadav S.Proteomic identification of Syzygium cumini seed extracts by MALDI-TOF/MS.Appl Biochem Biotechnol. 2014 Feb;172(4):2091-105.
Yadav VK, Mandal RS, Puniya BL, Singh S, Yadav S. Studies on the interactions of SAP-1 (an N-terminal truncated form of cystatin S) with its binding partners by CD-spectroscopic and molecular docking methods.J Biomol Struct Dyn. 2013 Nov 21. [Epub ahead of print]
Yadav VK, Chhikara N, Gill K, Dey S, Singh S, Yadav S.Three low molecular weight cysteine proteinase inhibitors of human seminal fluid: purification and enzyme kinetic properties.Biochimie. 2013 ;95(8):1552-9.
Tomar AK, Sooch BS, Raj I, Singh S, Yadav S.Interaction analysis identifies semenogelin I fragments as new binding partners of PIP in human seminal plasma. Int J Biol Macromol. 2013 Jan;52:296-9.
Chhikara N, Saraswat M, Tomar AK, Dey S, Singh S, Yadav S.Human epididymis protein-4 (HE-4): a novel cross-class protease inhibitor.PLoS One. 2012;7(11).
Tomar AK, Sooch BS, Singh S, Yadav S.Quantification studies in human seminal plasma samples identify prolactin inducible protein as a plausible marker of azoospermia.Biomarkers. 2012 Sep;17(6):545-51.
Tomar AK, Sooch BS, Singh S, Yadav S.Differential proteomics of human seminal plasma: A potential target for searching male infertility marker proteins. Proteomics Clin Appl. 2012 Apr;6(3-4):147-51.
Tomar AK, Sooch BS, Raj I, Singh S, Singh TP, Yadav S.Isolation and identification of Concanavalin A binding glycoproteins from human seminal plasma: a step towards identification of male infertility marker proteins.Dis Markers. 2011;31(6):379-86. 
Kumar S, Tomar AK, Singh S, Saraswat M, Singh S, Singh TP, Yadav S. Human serum albumin as a new interacting partner of prolactin inducible protein in human seminal plasma.Int J Biol Macromol. 2012 Mar 1;50(2):317-22.
 

Prof. Sujata Sharma

Prof. Sujata Sharma

 
Designation Professor
Email sujatasharma.aiims@gmail.com
Contact Number +91-11-26594608 ; +91-11-26593201
Research Interests Protein Structure Determination ; Rational Structure based Drug Design ; Multidrug Resistant Bacterial Therapeutics
Awards and Honors
National Bioscience Award for Career Development for the year 2011 (Department of Biotechnology, Govt. of India
National Woman Bioscientist Award for the year 2007 (Department of Biotechnology, Govt. of India) given by the President, Smt Pratibha Patil   
Best Poster Award in the 36th National Seminar in Crystallography, 2007 
Women Scientist of the Year 2006 (Biotech Research Society of India)
S V Talekar Medal for the best postgraduate of Department of Biophysics (AIIMS) for year 1998
Recent Significant Publications

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Sharma, S., Kaushik, S., Sinha, M., Singh, A., Sikarwar, J., Chaudhary, A., Gupta, A., Kaur, P. & Singh, T.P. (2014). Structural and functional insights into Peptidyl-tRNA Hydrolase. Biochem. Biophys. Acta.1844 : 1279-1288
Rastogi, N., Singh, A., Pandey, S.N., Sinha, M., Bhushan, A., Kaur, P., Sharma, S. & Singh, T.P. (2014). Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut. FEBS J. 281 : 2871-2882.  
Rastogi, R., Nagpal, N., Alam, N., Pandey, S., Gautam, L., Sinha, M., Shin, K., Manzoor, N., Virdi, J.S.,  Kaur, P., Sharma, S. & Singh, T.P.  (2014) Preparation and Antimicrobial Action of Three Tryptic Digested Functional Molecules of Bovine Lactoferrin. Plos One (2014)  9 : e90011.
Sharma, S., Sinha, M., Kaushik, S., Kaur, P. & Singh, T.P.  (2014). C-lobe of lactoferrin : The whole story of a half molecule. Biochem. Res. Int. (2013) Vol. 2013 : e271641.
Sharma, S., Singh, A.K., Kaushik, S., Sinha, M., Singh, R.P., Sharma, P., Sirohi, H.,  Kaur, P. & Singh, T.P. (2013) Lactoperoxidase : Stuctural Insights into Function, Ligand Binding and Inhibition. Int. J. Biochem. Mol. Biol. 4, 108-128.
Kaushik, S., Singh, N., Yamini, S., Singh, A., Sinha, M., Arora, A., Kaur, P., Sharma, S. & Singh, T.P. (2013). The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii. PLoS One. 8 : e67547.
Mir, R., Singh, N., Vikram, G., Kumar, R.P., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2009)). Structural basis of the prevention  NSAID-induced d amage of the gastrointestinal tract by C-terminal half (C-lobe)  of bovine colostrums protein lactoferrin: Binding andstructural studies of the C-lobe complexes with indomethacin, diclofenac, aspirin and ibuprofen. Biophys. J. 97, 3178-3186
Mir, R., Singh, N., Vikram, G.,  Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2010).  Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory Drugs (NSAIDs). Arch. Biochem. Biophy. 500, 196-202
Sharma, S., Jasti, J., Kumar. J., Mohanty, A.K. & Singh, T.P. (2003). Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9Å resolution.  J. Mol.  Biol. 321, 1286-1296. 
 

Ms. Asha Bhushan

Ms. Asha Bhushan

Designation

Scientist-IV

Email

यह ईमेल पता spambots से संरक्षित किया जा रहा है. आप जावास्क्रिप्ट यह देखने के सक्षम होना चाहिए. , यह ईमेल पता spambots से संरक्षित किया जा रहा है. आप जावास्क्रिप्ट यह देखने के सक्षम होना चाहिए.

Contact Number

+91-11-26594608, +91-11-26593201

Research Interests

 

Protein Structure Determination ; Data Collection and processing on High intensity X-Ray Beam, Cryocooling: Drug Design

Awards

 

 

 

 

 

 

 

 

 

Life Member of Indian Biophysical Society

Life Member of Indian Crystallographic Association

Life member of International Union of crystallography

Member of Asian Biophysical Society

Board Member of IJBST and its associated Journals http://ijbst.org

Selected for attending  "The XIX IUCr Congress and General Assembly in Geneva” 2002

The Outstanding scientist of the 21st century award by International Biographical Centre, Cambridge in 2007

Bursary for the 9th International conference on Biology and Synchrotron radiation from 13-17 August 2007  

Invited by  Prof. Kyriacos Petratos for  structure determination (BIOXIT) course in crystallography i

Selected for attending the CCP4 study weekend, 2010, East Midland, England.  

Honored with “Bharat Jyoti Award”  in the seminar “Economic Growth & National Integration”  by IIFS society on 26th March 2014 in New Delhi.

Selected as the outstanding scientist of the 21st century award by International Biographical Centre, Cambridge, England.; 2009

Recent Significant Publications

 

 

 

 

 

 

 

 

 

 

 

 

 

  

 

 

 

 

 

Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft. FEBS Open Bio. 2014 Oct 22;4:915-22. 

Singh A, Kumar A, Gautam L, Sharma P, Sinha M, Bhushan A, Kaur P, Sharma S, Arora A, Singh TP. (2014) Structural and binding studies of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa provide a platform for the structure-based inhibitor design against peptidyl-tRNA hydrolase. Biochem J. 463 : 329-37.

 

Rastogi N, Singh A, Pandey SN, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. (2014) Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut. FEBS J. 281:2871-82. 

 

Kumar S, Singh N, Sinha M, Dube D, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP.(2010): Crystal structure determination and inhibition studies of a novel xylanase and alpha-amylase inhibitor protein (XAIP) from Scadoxus multiflorus. FEBS J.: 277(13):2868-82. 

 

Mir, R., Singh, N., Vikram, G.,  Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2010).  Structural and binding studies of C-terminal half (C-lobe) of lactoferrin protein with COX-2-specific non-steroidal anti-inflammatory Drugs (NSAIDs). Arch. Biochem. Biophy.  500 , 196  - 202  

Mir R, Kumar RP, Singh N, Vikram GP, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP. (2010). Specific interactions of C-terminal half (C-lobe)  of lactoferrin protein with edible sugars: binding and structural studies with implications on diabetes.  Int J Biol Macromol.47,  50-9. 

Sheikh, I.A., Singh, A.K.,  Singh, N., Sinha, M., Singh, S.B., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2009). Structural evidence of substrate specificity in mammalian peroxidases: Structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4A resolution. J.  Biol.  Chem.  284, 14849  - 14856. . 

Singh, A.K., Kumar, R.P., Pandey, N.,  Singh, N., Sinha, M.,  Bhushan, A.,Kaur, P.,  Sharma, S.   &  Singh, T.P. (2009). Mode of binding of the tuberculosis prodrug isoniazid to peroxidases: Crystal structure of bovine lactoperoxidase with isoniazid at 2.7A resolution. J.  Biol.  Chem.  285  ,  1569 - 1576   

Mir, R., Singh, N., Vikram, G., Kumar, R.P., Sinha, M., Bhushan, A., Kaur, P., Srinivasan, A., Sharma, S. & Singh, T.P. (2009)). Structural basis of the prevention  NSAID-induced damage of the gastrointestinal tract by C-terminal half (C-lobe)  of bovine colostrums protein lactoferrin: Binding andstructural studies of the C-lobe complexes with indomethacin, diclofenac, aspirin and ibuprofen. Biophys.  J.  97,  3178 – 3186   

Singh, R.K., Ethayathulla, A.S., Jabeen, T.,  Sharma, S.,  Kaur, P.  &  Singh, T.P. (2005) . Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A2 : Crystal structure of the complex formed between phospholipase A2 and aspirin at 1.9 Å resolution.  J. Drug Target.  13 ,  113 – 119.  

 
 
 
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