Publications by authors named "Shalini Balakrishnan"

Arginine residues are broadly employed for specific biomolecular recognition, including in protein-protein, protein-DNA, and protein-RNA interactions. Arginine recognition commonly exploits the potential for bidentate electrostatic and hydrogen-bonding interactions. However, in arginine residues, the guanidinium functional group is located at the terminus of a flexible hydrocarbon side chain, which lacks the functionality to contribute to specific arginine-mediated recognition and may entropically disfavor binding.

View Article and Find Full Text PDF

Objectives/hypothesis: Reported here is a randomized retrospective analysis of 28 cases of elongated styloid process causing nagging cervicofacial pain, both unilateral and bilateral, and the effect of styloidectomy in these cases in relieving the symptom complex of the patient, in situations where conservative management failed in alleviating the symptoms.

Study Design: Randomized retrospective analysis over a period of 25 months.

Conclusion: Elongated styloid process causing glossopharyn-geal neuralgia is beginning to be a frequently encountered clinical entity nowadays.

View Article and Find Full Text PDF

Described here is a rare case of a craniopharyngioma of the nasopharynx and the sphenoid sinus and its surgical resection via an endoscopic, transnasal, transphenoidal approach. The study design is case report. Craniopharyngiomas are histologically benign, extra-axial slow growing tumours of the sellar and the supra sellar space.

View Article and Find Full Text PDF

To introduce chirality and functional groups adjacent to guanidiniums to modulate specificity and affinity in recognition, N,N'-bis(Boc)-alpha-guanidino acids were synthesized from alpha-amino acid methyl esters. Protected alpha-guanidino acids coupled to cyclohexylamine and trans-1,4-diaminocyclohexane in good yield and with retention of stereochemistry. Boc deprotection was conducted under mild acidic conditions (0.

View Article and Find Full Text PDF

Protein phosphorylation is a critical regulatory strategy. New tools are necessary which may be used to interrogate and are responsive to the activities of protein kinases and phosphatases. We have used protein design to develop a protein motif, termed a protein kinase-inducible domain, whose structure is dependent on its phosphorylation state.

View Article and Find Full Text PDF