Synthesis of Cyclic Disulfide Peptides: Comparison of Oxidation Methods. Pp. 157-164.
Jutta Eichler and Richard A. Houghten
[Abstract]
NMR Investigation of A Microtubule Binding Region Peptide from Human TAU Protein. Pp. 165-172.
Vesna de Serrano, Anthony A. Ribeiro, Warrren J. Strittmatter and Leonard D. Spicer
[Abstract]
SH-Group in the Active Site of alpha-Galactosidase from Trichodenna reesei. Pp. 173-180.
Elena V. Eneyskaya, Stepan V. Protasenya, Anatoly M. Kachurin, Andrew N. Savel'ev and Kirill N. Neustroev
[Abstract]
Cytocidal Activities of HIV-1 VPR and SAC1P Peptides Bioassayed in Yeast. Pp. 181-186.
L.G. Macreadie, A. Kirkpatrick, P.M. Strike and A.A. Azad
[Abstract]
Arginine and Peptidyl Oximes are Able to Inhibit Both Proprotein Convertases PC1 and Furin. Pp. 187-194.
Ajoy Basak and Claude Lazure
[Abstract]
Rapid and Efficient Purification of Rat Brain Dynamin Using an Affinity Column of the Carboxy-Terminal SH3 Domain of Grb2. Pp. 195-202.
José-Luis Montiel, Didier Cussac, Fabrice Cornille, Michel Vidal, Christiane Garbay and Bernard P. Roques
[Abstract]
Using Capillary Electrophoresis to Trace Hydrolysis of the Reactive Site Peptide Bond of Trypsin Inhibitors. Pp. 203-206.
Jan Rózycki, Piotr Mucha, Krzysztof Rolka and Piotr Rekowski
[Abstract]
Crystallisation Reports
Crystallization and Preliminary X-Ray Analysis of Mouse Pro-Renin Converting Enzyme. Pp. 207-210.
Michael Blaber
[Abstract]
Crystallization of a Hydrolase from Rhodococcus sp. Strain RHAl, the BphD Enzyme, in the PCB Degradation Pathway. Pp. 211-214.
N. Nandhagopal, Toshiya Senda, Takahashi Hatta, Akihiro Yamada, Eiji Masai, Masao Fukuda and Yukio Mitsui
[Abstract]
[Back to top] Striking Structural Resemblance Between Small Cysteine-Rich Proteins with Diverse Function. E.C. van Geerestein-Ujah, J.N. Breg, L. Sarda, P.J. Cozzone and R. Kaptein.
We have established a striking structural resemblance between the two domains of procolipase and several other small cysteine-rich proteins of diverse functions. The proteins share a common scaffold although the seuqence homology, apart from the cysteine pattern is quite low. The descriptions we delineate here should provide further constraints for use in the design of stable functional small proteins for pharmaceutical and chemical applications.
[Back to top] Synthesis of Cyclic Disulfide Peptides: Comparison of Oxidation Methods. Jutta Eichler and Richard A. Houghten.
Seven cyclic disulfide peptides (oxytocin, salmon calcitonin 1-10, CTP, crustacean cardioactive peptide, somatostatin 3-14, [C2,6]-beta-endorphin 1-6 and endothelin-beta 3-11) were synthesized on solid phase and cyclized either on the resin, simultaneously with the cleavage from the resin, or in solutions after cleavage, using eight different oxidatation methods. The purities of the crude peptides were compared in order to evalutate the efficacy of the different oxidation methods with respect to the peptide sequences.
[Back to top] NMR Investigation of A Microtubule Binding Region Peptide from Human TAU Protein. Vesna de Serrano, Anthony A. Ribeiro, Warrren J. Strittmatter and Leonard D. Spicer.
Solution NMR studies of tauD1, and 18-residue microtubule binding peptide from domain 1 of human tau protein, are reported. Using 2D 1H NMR (TOCSY, NOESY and ROESY) at 5 and 37ºC, we assigned the resonances fo almost all protons of tauD1 at pH 4.2, 5.8 and 7.3. While overall the peptide is highly disordered, several medium range NOE's give evidence for conformational preferences involving a gend at the T8-Q14 segment of the peptide.
[Back to top] SH-Group in the Active Site of alpha-Galactosidase from Trichodenna reesei. Elena V. Eneyskaya, Stepan V. Protasenya, Anatoly M. Kachurin, Andrew N. Savel'ev and Kirill N. Neustroev.
Modifications of an SH-group in active site of alpha-galactosidase from T. reesei by PHMB and HG2+ inactivate the enzyme while following treatment with thiols activity is recovered. Galactose and substrates delay such recovery. This effect was utilized to compare affinity of substrates and galactose to native and inactive forms of the enzyme. It was concluded that the SH-group is important for binding of substrates in the active site.
[Back to top] Cytocidal Activities of HIV-1 VPR and SAC1P Peptides Bioassayed in Yeast. L.G. Macreadie, A. Kirkpatrick, P.M. Strike and A.A. Azad.
Vpr is a protein of HIV-1 whose functions in viral replication has been uncertain. In this study we have determined that Vpr peptides containing the amino acid sequence HFRIGCRHSRIG are cytocidal when added externally to yeast cells in water, but not salt solutions. For the most effective toxidity, HFRIGCRHSRIG should be surrounded on each side by about eight amino acids from the native sequence. A peptide from the most similar cellular protein, Sac1p, also exhibited toxicity but at a five-fold weaker level.
[Back to top] Arginine and Peptidyl Oximes are Able to Inhibit Both Proprotein Convertases PC1 and Furin. Ajoy Basak and Claude Lazure.
Various Arginine derivatives bearing a modified carboxyl function as oxime, hydroxamate, N,O-dimethyl hydroxamate, O-methyl oxime and O-methyloxy carbonyl oxime were able to inhibit the enzymatic activities of hPC1 and hfurin towards a fluorescent peptidyl substrate. In an effort to improve the inhibition, a tetrapeptide containing a C-terminal arginine oxime, Arg-Lys-Lys-Arg-CH=NOH was prepared and, together with a side reaction product, Arg-Lys-Lys-Arg-C(NHOH)(OH)-N(OMe)Me, exhibited a much enhanced level of inhibition.
[Back to top] Rapid and Efficient Purification of Rat Brain Dynamin Using an Affinity Column of the Carboxy-Terminal SH3 Domain of Grb2. José-Luis Montiel, Didier Cussac, Fabrice Cornille, Michel Vidal, Christiane Garbay and Bernard P. Roques.
The carboxy-terminal SH3 domain of Grb2 coupled to sepharose gel was used to purify rat brain dynamin I. The affinity chromotography yielded two dynamin-rich fractions eluted with hight salt plus detergent and with low concentration of guanidinium-HCl, respectively. Both pools were purified to homogeneity using and ATP/agarose column and were shown by Far-Western blots and surface plasmon resonance (SPR) to have similar interactions with Grb2. The yield of this rapid purification procedure is significantly increased as compared to previously reported protocols.
[Back to top] Using Capillary Electrophoresis to Trace Hydrolysis of the Reactive Site Peptide Bond of Trypsin Inhibitors. Jan Rózycki, Piotr Mucha, Krzysztof Rolka and Piotr Rekowski.
Application of capillary electrophoresis for determination of the reactive site peptide bond hydrolysis in serine protease protein inhibitors by bovine beta-trypsin is reported in this paper. The advantage of this technique for such investigations has been underlined.
[Back to top] Crystallization and Preliminary X-Ray Analysis of Mouse Pro-Renin Converting Enzyme. Michael Blaber.
Hexagonal crystals (P6-4) of mouse pro-renin converting enzyme (PRECE) have been grown which diffract to better than 2.5Å. A native data set has been collected with 93% completion from 20 to 3.0Å. Using molecular replacement, with porcine kallikrein (PPK) as a search model (56% amino acid identity), a solution for a single molecule in the asymmetric unit has been identified. Refinement of the correctly positioned PPK model, against the PRECE dataset, has resulted in a PRECE model with an Rfactor of 24.7% and and Rfree of 32.8%.
[Back to top] Crystallization of a Hydrolase from Rhodococcus sp. Strain RHAl, the BphD Enzyme, in the PCB Degradation Pathway. N. Nandhagopal, Toshiya Senda, Takahashi Hatta, Akihiro Yamada, Eiji Masai, Masao Fukuda and Yukio Mitsui.
Crystals have been obtained for a 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic (HPDA) acid hydrolase (conventionally called as BphD) clone from Rhodococcus sp. strain RHA1. The crystals belonged to a tetrogonal space group (I422) and diffracted to 2.5Å.