منابع مشابه
Stabilization of gamma-turn conformations in peptides by disulfide bridging.
The ideal y-turn conformation in peptides is stabilized by the formation of two intramolecular hydrogen These are between the NH of residue i and the C=O of residue i + 2 (1 3, CJ and the C=O of residue i and the NH of residue i + 2 (3 1, C7).334 While this reverse-turn structural feature has been observed in proteins, '~~ unambiguous characterization of this conformation has yet to be realized...
متن کاملUnusually stable helix formation in short alanine-based peptides.
Short, 16-residue, alanine-based peptides show stable alpha-helix formation in H2O. This result is surprising when contrasted with the classical view that regards the alpha-helix as a marginally stable structure in H2O and considers short helices unstable. The alanine-based peptides are solubilized by insertion of three or more residues of a single charge type, lysine (+) or glutamic acid (-). ...
متن کاملThe polyproline II conformation in short alanine peptides is noncooperative.
The finding that short alanine peptides possess a high fraction of polyproline II (PII) structure (Phi=-75 degrees, Psi=+145 degrees ) at low temperature has broad implications for unfolded states of proteins. An important question concerns whether or not this structure is locally determined or cooperative. We have monitored the conformation of alanine in a series of model peptides AcGGAnGGNH2 ...
متن کاملCell adhesion molecule L1 in folded (horseshoe) and extended conformations.
We have investigated the structure of the cell adhesion molecule L1 by electron microscopy. We were particularly interested in the conformation of the four N-terminal immunoglobulin domains, because x-ray diffraction showed that these domains are bent into a horseshoe shape in the related molecules hemolin and axonin-1. Surprisingly, rotary-shadowed specimens showed the molecules to be elongate...
متن کاملElectric dipole moments and conformations of isolated peptides
The electric dipole moments of the isolated amino acid tryptophan and small glycine-based peptides (WGn, n = 1−5, W = tryptophan, G = glycine) have been measured by deflection of a molecular beam in an inhomogeneous electric field. The measurements are compared to the results of ab initio calculations and Monte-Carlo simulations. The conformation and the flexibility of the peptides, at differen...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2009
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.12.916