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Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis.
A computer modeling procedure for assessing the stereochemical suitability of pairs of residues in proteins as potential sites for introduction of cystine disulfide crosslinks has been developed and two positions for the introduction of 'stereochemically optimal' disulfides are identified in subtilisin. Expand
Conformations of disulfide bridges in proteins.
Disulfide bridging across antiparallel extended strands is observed in alpha-lytic protease, crambin, and beta-trypsin and this structure is shown to be very similar to those obtained in small cystine peptides. Expand
Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins
Mass spectrometric analysis of a banyan endophyte, Bacillus subtilis K1, extract revealed a complex mixture of lipopeptides, iturins, surfactins, and fengycins, where four major sites of heterogeneity are identified. Expand
Disallowed Ramachandran conformations of amino acid residues in protein structures.
An analysis of the nature and distribution of disallowed Ramachandran conformations of amino acid residues observed in high resolution protein crystal structures has been carried out and reveals instances of conservation of unusual stereochemistry. Expand
Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals.
An analysis on the nature of alpha-helix stop signals has been carried out, using a dataset of 1057 helices identified from 250 high resolution, non-homologous, protein crystal structures, and reveals that Pro residues flanked by polar amino acids have a very strong tendency to terminate helices. Expand
A model for the interaction of trifluoroethanol with peptides and proteins.
  • R. Rajan, P. Balaram
  • Chemistry, Medicine
  • International journal of peptide and protein…
  • 12 January 2009
A model is proposed for TFE interaction with peptides which involves an initial replacement of the hydration shell by fluoroalcohol molecules, a process driven by apolar interactions and favourable entropy of dehydration. Expand
Entrapment of a water wire in a hydrophobic peptide channel with an aromatic lining.
The structural model suggests that Grotthuss type proton conduction may, through constricted hydrophobic channels, be facilitated by concerted, rotational reorientation of water molecules. Expand
Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.
Structures in four different crystal forms of [Leu1]zervamicin, a membrane channel-forming polypeptide from Emericellopsis salmosynnemata, have been determined by x-ray diffraction, suggesting a gating mechanism for cation transport. Expand
Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant.
It is implied that the dissociation of the dimer into monomers ultimately leads to the collapse of the structure, suggesting that the interfacial interactions play a major role in determining multimeric protein stability. Expand