849925-49-1Relevant academic research and scientific papers
Analysis of designed β-hairpin peptides: Molecular conformation and packing in crystals
Aravinda, Subrayashastry,Raghavender, Upadhyayula S.,Rai, Rajkishor,Harini, Veldore V.,Shamala, Narayanaswamy,Balaram, Padmanabhan
, p. 4220 - 4231 (2013/07/25)
The crystal structures of several designed peptide hairpins have been determined in order to establish features of molecular conformations and modes of aggregation in the crystals. Hairpin formation has been induced using a centrally positioned D/su
Expanding the peptide β -turn in α γ hybrid sequences: 12 atom hydrogen bonded helical and hairpin turns
Chatterjee, Sunanda,Vasudev, Prema G.,Raghothama, Srinivasarao,Ramakrishnan, Chandrasekharan,Shamala, Narayanaswamy,Balaram, Padmanabhan
supporting information; experimental part, p. 5956 - 5965 (2009/09/24)
Hybrid peptide segments containing contiguous a and y amino acid residues can form C 12 hydrogen bonded turns which may be consideredas backbone expanded analogues of C 10 OS-turns) found in aa segments. Exploration of the regular hy
Differences arising in human neutrophil activation passing from N-formyl to N-acetyl-oligopeptides
Spisani, Susanna,Cavicchioni, Giorgio
, p. 252 - 259 (2007/10/03)
N-formyl- and N-acetyl-peptides were synthesized and compared in order to understand which features can best elicit biological responses. The behavior of N-formyl-peptides confirms the previously found sequential obligations in the residues, while acetyl-
