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Biomedical subjects

A Aubry

Publications and source records attributed to A Aubry.

60 records · Page 4Linked to original sources
PubMedDate not supplied

Crystal structure of the W35A mutant thioredoxin h from Chlamydomonas reinhardtii: the substitution of the conserved active site Trp leads to modifications in the environment of the two catalytic cysteines.

The conformational analysis of W35A thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii in the solid state has been carried out by x-ray diffraction, with the aim to clarify the role of Trp in the catalysis. Comparative analysis of W35A mutant with wild-type (WT) thioredoxin shows that, even if the structural motif of thioredoxin is not perturbed, the substitution of Trp35 by an Ala leads to significant changes in protein conformation near the active site. This rearrangement increases its solvent exposure and explains the change of the pKa values of the catalytic cysteines. The substitution of the Trp residue also influences the crystal packing as well as the recognition ability of thioredoxin. The solid state analysis suggests that the Trp residue has a structural function both to force the active site in the bioactive conformation, and to mediate the protein-protein recognition.

Amino Acid Substitution↗
PubMedDate not supplied

Folded structures in protonated reduced dipeptides.

Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R" (rXbb, reduced analogue of residue Xbb: NH-C alpha HR1-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i+2 or i+3-->i interaction. The resulting conformation is similar to the y- or beta-turn structure found in peptides and proteins.

Crystallization↗
PubMedDate not supplied

[Malignant melanoma of the gallbladder].

The authors present a case of secondary melanoma of the gallbladder, surgically discovered during a laparotomy for assumed biliary tract pathology. The primary tumor was a cutaneous melanoma at the right leg treated by surgery, four years before. At the laparotomy, the pancreas and the omentum contained also metastases. After cholecystectomy the cancerous evolution quickened and led to death after one year. The exceptional character of this observation lead the authors to review the literature.

Female↗
PubMedDate not supplied

(R)-isovaline homo-peptides adopt the left-handed 3(10)-helical structure.

A complete series of N- and C-blocked, monodispersed homo-oligopeptides from the sterically hindered (R)-isovaline residue to the hexamer level was synthesized step by step by solution methods and fully characterized. The preferred conformation of all the oligopeptides was determined in deuteriochloroform solution by Fourier transform infrared absorption and 1H nuclear magnetic resonance. In addition, the molecular structures of tripeptide, tetrapeptide and pentapeptide were assessed in the crystal state by x-ray diffraction. The results obtained confirm the conclusions from previous studies, namely that beta-bends and 3(10)-helices are preferentially adopted by isovaline-rich peptides, a clear indication that this C alpha, alpha-disubstituted glycine tends to induce folded structures much more extensively than its unmethylated parent compound alpha-aminobutyric acid. Furthermore, in this work we were able to demonstrate unambiguously for the first time that the relationship between isovaline chirality and helix screw sense is the same as that promoted by C alpha-monosubstituted glycines [(R)-amino acids give left-handed helical structures]. A comparison is also made with the conclusions extracted from published work on homo-oligopeptides from other C alpha-methylated amino acids.

Crystallography, X-Ray↗
PubMedDate not supplied

Synthesis and conformational analysis of (alpha Me)Leu/Aib model peptides.

We have synthesized by solution methods and fully characterized a variety of (alpha Me)Leu/Aib model peptides to the octapeptide level. A solution conformational analysis was performed by using infrared absorption. 1H nuclear magnetic resonance, and circular dichroism. The crystal-state structures of Z-D-(alpha Me)Leu-(Aib)2-OtBu, pBrBz-(Aib)2-D-(alpha Me)Leu-(Aib)2-OtBu, and Ac-(Aib)2-D-(alpha Me)Leu-(Aib)2-OtBu monohydrate were solved by x-ray diffraction. The results indicate that the (alpha Me)Leu residue may be easily incorporated into beta-bends and 3(10)-helical structures, and suggest that this residue tends to induce a helix handedness opposite to that promoted by its unmethylated counterpart (Leu) of the same optical configuration.

Aminoisobutyric Acids↗