Animesh Pramanik

An Unusual C–H . . . O Hydrogen Bond Mediated Reversal of Polypeptide Chain Direction in a Synthetic Peptide Helix (2000)

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...

An Unusual C–H . . . O Hydrogen Bond Mediated Reversal of Polypeptide Chain Direction in a Synthetic Peptide Helix (2000)

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...

\omega-Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a \beta-Alanyl-\gamma-Aminobutyryl Segment (1997)

Karle, IL, Pramanik, Animesh, Banerjee, Arindam, Bhattacharjya, Surajit, Balaram, P

Insertion of achiral \omega-amino acids into peptide sequences results in replacement of scissile peptide bonds by proteolytically stable C-C bonds. This provides a convenient means of creating...

Characterization of Helix Terminating Schellman Motifs in Peptides. Crystal Structure and Nuclear Overhauser Effect Analysis of a Synthetic Heptapeptide Helix (1997)

Datta, Saumen, Shamala, N, Banerjee, Arindam, Pramanik, Animesh, Bhattacharjya, Surajit, Balaram, P

The Schellman motif is a widely observed, helix terminating structural motif in proteins, which is achieved by the adoption of a left-handed helical (alphaL) conformation by a C-terminus residue. The...

\omega-Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a \beta-Alanyl-\gamma-Aminobutyryl Segment (1997)

Karle, IL, Pramanik, Animesh, Banerjee, Arindam, Bhattacharjya, Surajit, Balaram, P

Insertion of achiral \omega-amino acids into peptide sequences results in replacement of scissile peptide bonds by proteolytically stable C-C bonds. This provides a convenient means of creating...

Characterization of Helix Terminating Schellman Motifs in Peptides. Crystal Structure and Nuclear Overhauser Effect Analysis of a Synthetic Heptapeptide Helix (1997)

Datta, Saumen, Shamala, N, Banerjee, Arindam, Pramanik, Animesh, Bhattacharjya, Surajit, Balaram, P

The Schellman motif is a widely observed, helix terminating structural motif in proteins, which is achieved by the adoption of a left-handed helical (alphaL) conformation by a C-terminus residue. The...

Omega Amino Acids in Peptide Design: Incorporation into Helices (1996)

Banerjee, Arindam, Pramanik, Animesh, Bhattacharjya, Surajit, Balaram, P

Incorporation of easily available achiral omega-amino acid residues into an oligopeptide results in substitution of amide bonds by polymethylene units of an aliphatic chain, thereby providing a...

Omega Amino Acids in Peptide Design: Incorporation into Helices (1996)

Banerjee, Arindam, Pramanik, Animesh, Bhattacharjya, Surajit, Balaram, P

Incorporation of easily available achiral omega-amino acid residues into an oligopeptide results in substitution of amide bonds by polymethylene units of an aliphatic chain, thereby providing a...

Heterogeneity and Stability of Helical Conformations in Peptides: Crystallographic and NMR Studies of a Model Heptapeptide (1996)

Banerjee, Arindam, Datta, S, Pramanik, Animesh, Shamala, N, Balaram, P

The helix is a common secondary structural element in proteins. Several subtypes of helical structures are possible, depending on the nature of the backbone hydrogen-bonding pattern. For short...

Heterogeneity and Stability of Helical Conformations in Peptides: Crystallographic and NMR Studies of a Model Heptapeptide (1996)

Banerjee, Arindam, Datta, S, Pramanik, Animesh, Shamala, N, Balaram, P

The helix is a common secondary structural element in proteins. Several subtypes of helical structures are possible, depending on the nature of the backbone hydrogen-bonding pattern. For short...