S. Agarwalla

Possible Ion Channel Model in Crystals of Leu-Zervamicin, (9999)

Karle, I. L., Flippen-Anderson, J. L., Agarwalla, S., Balaram, P.

The best-studied members of this class are the alamethicins for which a crystal structure has been reported. The conformation of the peptide molecule was established to be a bent helix; however, the...

Conformation of the Flexible Bent Helix of Leu 1-Zervamicin in Crystal C and a Possible Gating Action for Ion Passage (1994)

Karle, Isabella L, Flippen-Anderson, Judith L, Agarwalla, S, Balaram, P

The membrane channel-forming polypeptide, Leu '-zervamicin, Ac-Leu-Ile-Gln-ha-Ile5-Thr-Aib-Leu-Aib-Hyp'o-Gln-Aib-Hyp-Aib-Pro'5-Phol ( Aib: a-aminoisobutyric acid; Iva: isovaline; Hyp:...

Conformation of the Flexible Bent Helix of Leu 1-Zervamicin in Crystal C and a Possible Gating Action for Ion Passage (1994)

Karle, Isabella L, Flippen-Anderson, Judith L, Agarwalla, S, Balaram, P

The membrane channel-forming polypeptide, Leu '-zervamicin, Ac-Leu-Ile-Gln-ha-Ile5-Thr-Aib-Leu-Aib-Hyp'o-Gln-Aib-Hyp-Aib-Pro'5-Phol ( Aib: a-aminoisobutyric acid; Iva: isovaline; Hyp:...

Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.

Karle, I L, Flippen-Anderson, J L, Agarwalla, S, Balaram, P

Structures in four different crystal forms of [Leu1]zervamicin (zervamicin Z-L, Ac-Leu-Ile-Gln-Iva-Ile5-Thr-Aib-Leu-Aib-Hyp10-Gln-Aib-Hyp-Aib-P ro15-Phol, where Iva is isovaline, Aib is alpha-amino...

Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.

Karle, I L, Flippen-Anderson, J L, Agarwalla, S, Balaram, P

Structures in four different crystal forms of [Leu1]zervamicin (zervamicin Z-L, Ac-Leu-Ile-Gln-Iva-Ile5-Thr-Aib-Leu-Aib-Hyp10-Gln-Aib-Hyp-Aib-P ro15-Phol, where Iva is isovaline, Aib is alpha-amino...

Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase.

Agarwalla, S., Gokhale, R. S., Santi, D. V., Balaram, P.

Thymidylate synthase (TS), a dimeric enzyme, forms large soluble aggregates at concentrations of urea (3.3-5M), well below that required for complete denaturation, as established by fluorescence and...