JPP40 tendency to acquire helical conformation in helix inducing, solvent 2,2,2- trifluoroethanol. Overall the increase in cationic charge of a-MSH improved Staphylocidal activity and membrane damaging efficacy of the peptides without compromising their cell selectivity. It also indicated that electrostatic interactions and ability to acquire ordered conformation may be crucial for a-MSH_ and its analogues to selectively disrupt microbial membrane leading to bacterial cell death without harming host cell membrane. Structure based Function Prediction of Hypothetical Proteins from Neisseria gonorrhoeae oP 21 Kundan Kumar, Amresh Prakash, Asimul Islam, Faizan ‘Ahmad, and Md. Imtaiyaz Hassan’ Centre for Interdisciplinary Research in Basic Sciences Islamia, New Dethi-110025, India Jamia Mitta Neisseria gonorrhoeae is a Gram-negative bacteria predominantly causes a sexually transmitted infection known as gonorrhoea. The frequent emergence of new multiple drug resistant strain need the extensive study of its genome and development of new drug/ vaccine against these pathogen. After analysis of the proteome data of N. gonorrhoeae we found that a large fraction proteome are listed as conserved hypothetical protein (HP) for which function are still not known. Study of these HPs offers presentation of new structures and novel functions of HPs and also new cascade of biochemical pathways. Furthermore, new HPs may be serving as ‘markers and pharmacological targets. We have identited 10 HPs showing lyases activity from N. gonorrhoeae from sequence analysis and performed homology modeling to reveal the structural basis of the function, structural motifs and amino acids involved in catalytic sites. Along with this, function may be inferred on the basis of properties that are associated with a specie functional class and family of the proteins. We also studied the sub- cellular localization and presence of signal peptide in the HPs, Moreover, sequence analysis was also performed to find out the physicochemical properties including ‘amino acid composition, aliphatic index and instability index of HPs. Finally, function annotation and identidcation of functionally important regions in HPs from N. gonorrhoeae may leads to better understanding of its virulence mechanism, adaptability in host system, tolerance for host immune system and emergence of drugs resistance strain and finally drug/vaccine discovery. ~ E-mail: mihassan@jmi.ac.in Study of dynamics of Protein Nanoparticle complex in aqueous medium using Impedance spectroscopy op 22 Mahesh Samant, Bipin Khade, H Muthurajan* P M Dongre Department of Biophysics, University of Mumbai, Santacruz (E), Muni 400098 *National Centre for Nanosciences and Nanotechnology, University of Mumbai, Mumbai 400098 A rapid development of nanosciences and nanotechnology offers nanoparticles great applications in various fields, like drug development, materials for drug delivery and biosensors etc. Nanoparticles possesses a unique physicho-chemical properties such as optical, ‘magnetic, large surface to volume ratio etc. Nanoparticles also confer properties of enhanced bioavailability and improved solubility. When nanoaprticles enters in biological fluids, it leads undesired effects. The effects ‘may or may not favour to the systems. Hence itis prime important to understand interaction between nanoaprticles and biological materials like proteins, ‘enzymes and nucleic acids etc. In the present investigation we studied the nanoparticle- protein complex using dielectric spectroscopy. Dielectric spectroscopy reveals typical signature of relaxation process of aqueous media namely dielectric constant, dielectric loss which commonly known as a, B, y and 8 relaxation. ‘The Chemical route synthesized Silver Nanoparticles were characterized using Dynamic Light Scattering (DLS), Transmission Electron Microscope (TEM) and UV visible spectroscopy. The protein nanoparticles complex was confirmed by fluorescence and UV visible spectroscopy. The Frequency dependent Dielectric dispersion of Silver NP’s and Silver NP-protein complex was investigated in the temperature range of 263K ~ 373K and in a frequency range of 20Hz - 2MHz by impedance spectroscopy (Agilent LCR component analyzer). Variation in dielectric constant (2’) and dielectric loss (e”) was observed nanopartilce and protein and Protein-nanoaparticle complex. Bode plot (impedance vs frequency) showed increased in impedance (Z) of protein-npts complex. ‘Average relaxation time (x) for a-region (20HZ-100KHZ) and B-region ( > 200 KHZ) was tabulate in control and test condition as a function of reciprocal temperature. In addition, the electrical conductivity was monitored. The several relaxation processes were attributed to motions that range from side groups of the proteins in the aqueous medium, E-mail: samant.mahesh77@gmail.com