Biomedical subjects

K Lala

Publications and source records attributed to K Lala.

3 recordsLinked to original sources

PubMed1994

Purification, N-terminal sequence and structural characterization of a toxic protein from the Indian scorpion venom Buthus tamulus.

A toxic protein component (Bt-II) was isolated from the venom of the Indian scorpion, Buthus tamulus, by ion-exchange chromatography on Biorex-70 and reverse phase high pressure liquid chromatography (RP-HPLC). This 7800 mol. wt protein was found to have an LD50 value of 2.25 mg/kg body weight in mice by subcutaneous injection. Amino acid composition of the protein revealed the presence of aromatic and basic amino acids; the N-terminal amino acid sequence was also determined. Structural characterization of Bt-II, based on circular dichroic and fluorescent quenching studies, has also been reported.

Amino Acid Sequence↗

PubMed1992

Prediction of tertiary structures in 'scorpion-toxin' type proteins.

In the three-dimensional architecture of macromolecules, the structural stability and proper folding manifest due to cooperative packing interaction of various segments. Hydrophobicity is the major factor stabilizing protein-protein associations. In the disulfide-containing proteins, S-S bonds are integral part of structural motifs and large part of the protein-folding problem can be reduced to identifying and understanding motifs and subdomains of these proteins. Identifying such a motif with S-S bonds in 'scorpion-toxin' type proteins, and from model-building studies, five tertiary structural models for these type of proteins can be proposed. These canonical structural models can be refined by regular minimum energy and computer simulation methods to arrive at the final tertiary structures. Such 'models' can be of considerable use i) in understanding the biochemical reaction mechanisms in the structure-function relationships, ii) structure determination by X-ray methods (molecular replacement method), iii) drug design etc.

Amino Acid Sequence↗

PubMed1976

Conformational dependence on pH in tripeptides.

From the 1H-NMR study of Tyr-Gly-Gly and Phe-Gly-Gly in H2O and 2H2O as a function of pH it follows that these tripeptides display at least two and probably three conformational zones. Under slow exchange conditions of the peptidic NH-protons, coupling constants 3J(NH, CaH) may be extracted as the probe. At higher pH values shift values and 3J(a, beta) of the side chain and the titration curves are indicative for these conformational alterations.

Glycine↗