Aravinda, Subrayashastry, Harini, Veldore Vidya, Shamala, Narayanaswamy, Das, Chittaranjan, Balaram, Padmanabhan
De noVo designed ‚b-hairpin peptides have generally been recalcitrant to crystallization. The crystal structures of four synthetic peptide ‚b-hairpins, Boc-Leu-Val-Val-DPro-Gly-Leu-Phe-Val-OMe...
Aravinda, Subrayashastry, Shamala, Narayanaswamy, Das, Chittaranjan, Sriranjini, Arumugam, Karle, Isabella L, Balaram, Padmanabhan
Aromatic-aromatic interactions between phenylalanine side chains in peptides have been probed by the structure determination in crystals of three peptides: Boc-Val-Ala-Phe-Aib-Val-Ala-Phe-Aib-OMe, I;...
Structural Analysis of Peptide Helices Containing Centrally Positioned Lactic Acid Residues (2002)
Aravinda, S, Shamala, N, Das, Chittaranjan, Balaram, P
The effect of insertion of lactic acid (Lac) residues into peptide helices has been probed using specifically designed sequences. The crystal structures of 11-residue and 14-residue depsipeptides...
Karle, Isabella L, Das, Chittaranjan, Balaram, P
The insertion of alpha-hydroxy acids into peptide chains provides a convenient means for investigating the effects of hydrogen bond deletion on polypeptide secondary structures. The crystal...
Designed beta-Hairpin Peptides with Defined Tight Turn Stereochemistry (2001)
Das, Chittaranjan, Naganagowda, GA, Karle, Isabella L, Balaram, P
The conformational analysis of two synthetic octapeptides, Boc–Leu–Val–Val–D-Pro–L-Ala–Leu–Val–Val–OMe (1) and Boc–Leu–Val–Val–D-Pro–D-Ala–Leu–Val–Val–OMe (2) has...
Molecular Carpentry: Piecing Together Helices and Hairpins in Designed Peptides (2001)
Das, Chittaranjan, Shankaramma, Channaveerappa S, Balaram, Padmanabhan
The design of a peptide that contains two distinct elements of secondary structure, helix and beta-hairpin, is described. Two designed 17-residue peptides:...
Designed β-Hairpin, β-Sheet And Mixed α-β Structures In Synthetic Peptides (2000)
Synthetic construction of protein molecules has been widely pursued over the last two decades. A primary goal behind de novo protein design has been to build minimal systems by capturing the...
Designed β-Hairpin, β-Sheet And Mixed α-β Structures In Synthetic Peptides (2000)
Synthetic construction of protein molecules has been widely pursued over the last two decades. A primary goal behind de novo protein design has been to build minimal systems by capturing the...
Designed β-Hairpin, β-Sheet And Mixed α-β Structures In Synthetic Peptides (2000)
Synthetic construction of protein molecules has been widely pursued over the last two decades. A primary goal behind de novo protein design has been to build minimal systems by capturing the...
Aravinda, S, Shamala, N, Pramanik, Animesh, Das, Chittaranjan, Balaram, P
An unusual C-terminal conformation has been detected in a synthetic decapeptide designed to analyze the stereochemistry of helix termination in polypeptides. The crystal structure of the decapeptide...
Karle, Isabella L, Das, Chittaranjan, Balaram, Padmanabhan
The Meccano (or Lego) set approach to synthetic protein design envisages covalent assembly of prefabricated units of peptide secondary structure. Stereochemical control over peptide folding is...
Vibrational Circular Dichroism of beta-Hairpin Peptides (2000)
Zhao, Chunxia, Polavarapu, Prasad L, Das, Chittaranjan, Balaram, P
Analysis of vibrational absorption and vibrational circular dichroism (VCD) for synthetic peptides designed to adopt beta-hairpin conformations reveals characteristic well-resolved amide I absorption...
A four stranded beta-sheet structure in a designed, synthetic polypeptide (1999)
Das, Chittaranjan, Raghothama, S, Balaram, P
A designed four stranded beta-sheet peptide has been constructed using three internal d-proline residues to nucleate beta-hairpin formation.
A Designed Three Stranded beta-Sheet Peptide as a Multiple beta-Hairpin Model (1998)
Das, Chittaranjan, Raghothama, S, Balaram, P
Beta-Hairpins are important elements in protein structure,1 implicated in the nucleation of beta-sheets in protein folding.2 Multiple hairpin structures, in which successive strands are connected by...
Karle, Isabella L., Das, Chittaranjan, Balaram, Padmanabhan
The Meccano (or Lego) set approach to synthetic protein design envisages covalent assembly of prefabricated units of peptide secondary structure. Stereochemical control over peptide folding is...
The initial substrate-binding site of γ-secretase is located on presenilin near the active site
Kornilova, Anna Y., Bihel, Frédéric, Das, Chittaranjan, Wolfe, Michael S.
γ-Secretase is a structurally enigmatic multiprotein complex that catalyzes intramembrane proteolysis of a variety of substrates, including the amyloid β-protein precursor of Alzheimer's disease...
Das, Chittaranjan, Hoang, Quyen Q., Kreinbring, Cheryl A., Luchansky, Sarah J., Meray, Robin K., Ray, Soumya S., ...
The ubiquitin C-terminal hydrolase UCH-L1 (PGP9.5) comprises >1% of total brain protein but is almost absent from other tissues [Wilkinson, K. D., et al. (1989) Science 246, 670–673]. Mutations in...
Karle, Isabella L., Das, Chittaranjan, Balaram, Padmanabhan
The Meccano (or Lego) set approach to synthetic protein design envisages covalent assembly of prefabricated units of peptide secondary structure. Stereochemical control over peptide folding is...
The initial substrate-binding site of γ-secretase is located on presenilin near the active site
Kornilova, Anna Y., Bihel, Frédéric, Das, Chittaranjan, Wolfe, Michael S.
γ-Secretase is a structurally enigmatic multiprotein complex that catalyzes intramembrane proteolysis of a variety of substrates, including the amyloid β-protein precursor of Alzheimer's disease...
Das, Chittaranjan, Hoang, Quyen Q., Kreinbring, Cheryl A., Luchansky, Sarah J., Meray, Robin K., Ray, Soumya S., ...
The ubiquitin C-terminal hydrolase UCH-L1 (PGP9.5) comprises >1% of total brain protein but is almost absent from other tissues [Wilkinson, K. D., et al. (1989) Science 246, 670–673]. Mutations in...