We found that high prevalence of MetS was NSC-737664 primarily indicated by central obesity combined with dyslipidemia (low HDL, Hypertension and triglycerides). The high prevalence of hypertriglyceridemia, notably in men, might be due to the sedentary lifestyle. This finding was contrary to the previous report.[11] CONCLUSION Our results suggest that prevalence of MetS was observed in non-obese patients and was higher in male patients and positively correlated with aging. Nevertheless, further studies are required to validate the MetS in larger population. ACKNOWLEDGMENTS We thank the diabetic patients of MGM hospital who participated in this study. We also thank Dr. M. Satyadev, Superintendent, Mahatma Gandhi Memorial Hospital, for his valuable suggestion and guidance to complete this pilot study.

Footnotes Source of Support: Nil Conflict of Interest: None declared
An ��-helix possesses a dipole moment by virtue of the alignment of its peptide bonds having half-positive and negative charges at their ends. For this fractional charge separation, a single peptide unit behaves like a microdipole.[1] When these microdipoles align along the axis of the ��-helix, making hydrogen bonds with the neighboring peptide units, the ��-helix behaves like a macrodipole with positive C-terminal and negative N-terminal on either end. The length[1] and the dipole moment () of an ��-helix macrodipole is 1.5N �� and 3.5N Debye, respectively, where N is the number of residues of the alpha helix.[2] Several groups have suggested that the ��-helix macrodipole can stabilize certain conformations of the protein.

[3,4] The structure and function of different voltage-gated potassium (K+) ion channels have been reviewed.[5] The transmembrane subunits of the channel comprise six ��-helices. The structure of voltage-gated K+ ion channel of Aeropyrum pernix (KvAP) obtained by different methods[6�C8] shows that, in a single subunit, the ��-helices are not ideally antiparallel but organized in a pairwise fashion, i.e., S1-S2, S3-S4, and S5-S6. The first four helices (S1, S2, S3, and S4) collectively are called the voltage sensor domain (VSD), the remaining (S5, S6) being pore domain (PD). The S3 helix has a kink at Proline P99, dividing it into two distinct helices S3a and S3b. S3b pairs with S4, forming a tightly bound ��paddle�� unit shuttling in and out of the membrane.

[9] S3b and S4 form a somewhat antiparallel macrodipole pair.[6�C8] Taking S3b and S4 ��-helices of the full-length K+ ion channel of KvAP (PDB 1ORQ)[6], the 14-residue (A100-L113) S3b ��-helix is 21 , while the 17-residue (R117- R133) S4 ��-helix is 25.5 long. The terminal dipole charges of S3b and S4 macrodipoles are N3 (positive), C3 (negative) and N4 (positive), C4 (negative), Drug_discovery respectively. Besides these charges, the ��-helices have a number of charged residues on their surfaces.