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DNA enriched for supercoiled plasmids prepared from the 3 micron plasmid-enriched, [psi+], [2 micron degrees] strain 6-1G-P188 and from the [2 micron+] [psi+] strain LL20 can be used to transform a psi- recipient strain to psi+. Fractionation of the former preparation by electrophoresis showed that the 3 micron plasmid band contained the transforming activity.
[reaction: see text] Acyclic psi[(E)-CH=CMe]- and psi[(Z)-CH=CMe]-type dipeptide isosteres were efficiently synthesized. In a key reaction, alpha-alkylation of gamma-mesyloxy-beta-methyl-alpha,beta-unsaturated esters with organocyanocuprates in diethyl ether or tetrahydrofuran preferentially afforded the psi[(E)-CH=CMe]- or psi[(Z)-CH=CMe]-isomer, respectively, via anti-S(N)2' mechanism.
We observe signals for the decays psi(3770) --> XJ/psi from data acquired with the CLEO detector operating at the CESR e+ e- collider with square root of s = 3773 MeV. We measure the following branching fractions Beta(psi(3770) --> XJ/psi and significances: (189 +/- 20 +/- 20) x 10(-5) (11.6sigma) for X = pi+ pi-, (80 +/- 25 +/- 16) x 10(-5) (3.4sigma) for X = pi0 pi0, and (87 +/- 33 +/- 22) x 10(-5) (3.5sigma) for X = eta, where the errors are statistical and systematic, respectively. The radiative return process e+ e- --> gamma psi(2S) populates the same event sample and is used to measure Gamma ee[psi(2S)] = (2.54 +/- 0.03 +/- 0.11) keV.
The core of the photosystem-I reaction center is formed by polypeptides PSI-A and PSI-B, the products of the homologous psaA and psaB genes. Based on hydropathy analyses, models have been proposed for the folding of these polypeptide chains in the membrane [Fish, L. E., Kück, U. & Bogorad, L. (1985), in Molecular biology of the photosynthetic apparatus, pp. 111-120, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY]. To test these models, we have tried to identify regions of PSI-A that are exposed to the surrounding medium, on the stromal or lumenal surface of the membrane. Immunogold labeling of thylakoid vesicles, with antibodies to synthetic peptides, shows that residues 413-421 of PSI-A are exposed on the stromal surface of the membrane, and that the accessibility of this region is enhanced by NaSCN treatment, which removes extrinsic polypeptides. This treatment also enhances a trypsin-cleavage site which may lie just after residues 413-421. Immunogold labeling also indicates that residues 371-379 and 497-505 are exposed on the lumenal surface. These results establish the conformation of the central portion of the polypeptide. Assuming that the transmembrane regions are correctly predicted by the 11-helix model, the N-terminal domain, as well as the conserved region proposed to bind the iron-sulfur center FX, would be expected to be on the stromal surface.
X-ray crystallography has been used to determine the 3D structures of two complexes between Streptomyces griseus proteinase B (SGPB), a bacterial serine proteinase, and backbone variants of turkey ovomucoid third domain (OMTKY3). The natural P1 residue (Leu18I) has been substituted by a proline residue (OMTKY3-Pro18I) and in the second variant, the peptide bond between Thr17I and Leu18I was replaced by an ester bond (OMTKY3-psi[COO]-Leu18I). Both variants lack the P1 NH group that donates a bifurcated hydrogen bond to the carbonyl O of Ser214 and O(gamma) of the catalytic Ser195, one of the common interactions between serine proteinases and their canonical inhibitors. The SGPB:OMTKY3-Pro18I complex has many structural differences in the vicinity of the S1 pocket when compared with the previously determined structure of SGPB:OMTKY3-Leu18I. The result is a huge difference in the DeltaG degrees of binding (8.3 kcal/mol), only part of which can be attributed to the missing hydrogen bond. In contrast, very little structural difference exists between the complexes of SGPB:OMTKY3-psi[COO]-Leu18I and SGPB:OMTKY3-Leu18I, aside from an ester O replacing the P1 NH group. Therefore, the difference in DeltaG degrees, 1.5 kcal/mol as calculated from the measured equilibrium association constants, can be attributed to the contribution of the P1 NH hydrogen bond toward binding. A crystal structure of OMTKY3 having a reduced peptide bond between P1 Leu18I and P'1 Asp19I, (OMTKY3-psi[CH2NH2+]-Asp19I) has also been determined by X-ray crystallography. This variant has very weak association equilibrium constants with SGPB and with chymotrypsin. The structure of the free inhibitor suggests that the reduced peptide bond has not introduced any major structural changes in the inhibitor. Therefore, its poor ability to inhibit serine proteinases is likely due to the disruptions of the canonical interactions at the oxyanion hole.
The decay of Psi' --> Psi + pipi is described by a chiral epsilon model. The general features of the observed dipion spectrum are well reproduced. Comparison with the hadronic decay rho' --> rho + pipi indicates that the Psi'Psiepsilon coupling is relatively suppressed by a factor approximately 10(-2).
The [psi] factor of yeast is cytoplasmically inherited. Singh, Helms and Sherman (1979) reported that high concentrations of KCl and of ethylene glycol induce the genetic change from [psi+] to [psi-]. In this study, the following agents have been shown to induce the same genetic change: guanidine hydrochloride at 1 mM, dimethyl sulfoxide at 2.5% v/v and ethanol or methanol at 10% v/v. It is likely that a number of other agents also cause the change, namely 2 M glycerol, M succinate, M glutamate and M MgCl2. Most of these agents induce the change at very high frequencies; with some, the frequency is 100%. Although the observed phenotypic change can also occur as a result of chromosomal gene mutation, no changes of this type were identified. Some of the agents also cause mutation from [rho+] to [rho-] and from killer to sensitive.
The peptide CO-NH function was replaced by a trans carbon-carbon double bond or by a CH2-CH2 isostere in enkephalin analogues of DADLE, DCDCE-NH2 or DPDPE. In DADLE the 2-3 and the 3-4 peptide bond was modified, whereas in the cyclic analogues the Gly3-Phe4 bond was replaced by the isosteres Gly psi (E,CH = CH)Phe [5-amino-2-(phenylmethyl)-3(E)-pentenoic acid] or Gly psi (CH2CH2)Phe [5-amino-2-(phenylmethyl)pentanoic acid]. In general, the modification results in a drop in potency which is the largest for the flexible CH2-CH2 replacement. The Gly3 psi (E,CH = CH)Phe4 DCDCE-NH2 analogue retains considerable potency. These results confirm the importance of the peptide function at the 2-3 and 3-4 position in enkephalin analogues for biological potency.
Treatment of 3'-5'-O-(1,1,3,3-tetraisopropyldisiloxanyl)-1,3-dimethyl-psi-uridine (7) . with one equivalent of base and a slight excess of trifluoromethanesulfonic anhydride afforded 5'-O-trifluoromethanesulfonyl-2',3'-O-(1, 1,3,3-tetraisopropyldisiloxanyl)-1,3-dimethyl-psi-uridine (8). Nucleophilic displacement of the 5'-trifluoromethanesulfonyloxy group by treatment with various alkali metal salts of halide, azide, or acetate followed by deprotection by fluoride ion treatment afforded the corresponding 5'-substituted-1, 3-dimethyl-psi-uridine derivatives (10) in good yields in crystalline form.
The solid state conformations of cyclo [Gly-Pro psi[CH2S] Gly-D-Phe-Pro] and cyclo [Gly-Pro psi[CH2-(S)-SO]Gly-D-Phe-Pro] have been characterized by X-ray diffraction analysis. Crystals of the sulfide trihydrate are orthorhombic, P2(1)2(1)2(1), with a = 10.156(3) A, b = 11.704(3) A, c = 21.913(4) A, and Z = 4. Crystals of the sulfoxide are monoclinic, P2(1) with a = 10.662(1) A, b = 8.552(3) A, c = 12.947(2) A, beta = 94.28(2), and Z = 2. Unlike their all-amide parent, which adopts an all-trans backbone conformation and a type II beta-turn encompassing Gly-Pro-Gly-D-Phe, both of these peptides contain a cis Gly1-Pro2 bond and form a novel turn structure, i.e., a type II' beta-turn consisting of Gly-D-Phe-Pro-Gly. The turn structure in each of these peptides is stabilized by an intramolecular H bond between the carbonyl oxygen of Gly1 and the amide proton of D-Phe4. In the cyclic sulfoxide, the sulfinyl group is not involved in H bonding despite its strong potential as a hydrogen-bond acceptor. The crystal structure made it possible to establish the absolute configuration of the sulfinyl group in this peptide. The two crystal structures also helped identify a type II' beta-turn in the DMSO-d6 solution conformers of these peptides.
Since the founding of the Society of Psychical Research in 1982, psychical researchers have, in each generation, generated research reports which they believed justified the existence of paranormal phenomena. Throughout this period the scientific establishment has either rejected or ignored such claims. The parapsychologists, with some justification, complained that their claims were being rejected without the benefit of a fair hearing. This paper asks the question of how well the best contemporary evidence for psi--the term used to designate ESP and psychokinetic phenomena--stands up to fair and unbiased appraisal. The results of the scrutiny of the three most widely heralded programs of research--the remote viewing experiments, the psi ganzfeld research, and the work with random number generators--indicates that parapsychological research falls short of the professed standards of the field. In particular, the available reports indicate that randomization is often inadequate, multiple statistical testing without adjustment for significance levels is prevalent, possibilities for sensory leakage are not uniformly prevented, errors in use of statistical tests are much too common, and documentation is typically inadequate. Although the responsible critic cannot argue that these observed departures from optimal experimental procedures have been the sole cause of the reported findings, it is reasonable to demand that the parapsychologists produce consistently significant findings from experiments that are methodologically adequate before their claims are taken seriously.
[reaction: see text] A straightforward synthetic route for the synthesis of diastereomerically pure psi[(E)-CMe=CH]- and psi[(E)-CMe=CMe]-type dipeptide isosteres was developed on the basis of regio- and stereoselective anti-S(N)2' alkylation of 3-(N-Boc-5-methyl-4-substituted-oxazolidin-2-on-5-yl)acrylates with organocopper reagents.
Using data collected with the CLEO detector operating at the CESR e+e- collider at sqrt[s]=3.97-4.26 GeV, we investigate 15 charmonium decay modes of the psi(4040), psi(4160), and Y(4260) resonances. We confirm, at 11 sigma significance, the BABAR Y(4260)-->pi+pi- J/psi discovery, make the first observation of Y(4260)--> pi(0)pi(0) J/psi (5.1 sigma), and find the first evidence for Y(4260)-->K+K- J/psi(3.7 sigma). We measure e+e- cross sections at sqrt[s]=4.26 GeV as sigma(pi+pi- J/psi)=58(+12)(-10)+/-4 pb, sigma(pi(0)pi(0) J/psi)=23(+12)(-8)+/-1 pb, and sigma(K+K- J/psi)=9(+9)(-5)+/-1 pb, in which the uncertainties are statistical and systematic, respectively. Upper limits are placed on other decay rates from all three resonances.
The intact photosystem I of maize containing its full antenna complement (PSI-200) has been purified and fractionated into the core and outer antenna (LHCI) components. It is demonstrated by absorption and fluorescence spectroscopy that at least 80% of the long wavelength absorbing antenna pigments (red forms) are located in LHCI. Absorption spectra in the Qy region of all three preparations were measured between 72 and 300 K and subjected to a thermal broadening analysis. Data are interpreted in the linear electron-phonon coupling assumption, and the average optical reorganization energy (Snum) for the bulk pigment band and the red absorption tail determined. A marked asymmetry in Snum values across the absorption band is demonstrated. The bulk pigments in all three preparations have rather low values, in the range of 15-25 cm-1, suggesting that Stokes shifts for the absorption forms are in the 1. 5-3 nm range. On the other hand the red forms have markedly greater reorganization energies. While a direct thermal analysis of the red tail indicates minimum Snum values of around 60 cm-1, when the contribution of the red tail of the bulk pigments is corrected for in LHCI, the more reliable value of 110 cm-1 is obtained. These high Snum values for the red pigment forms suggest that they have unusually wide homogeneously broadened absorption bands and large Stokes shifts (6-11 nm).
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An efficient purification of synthetic all-trans (all-E) lycophyll is described. The synthetic preparation of the rare xanthophyll lycophyll produces a mixture of geometric isomers. Purification by HPLC using reverse-phase C30 silica affords milligram quantities of the desired all-trans isomer in >95% purity, as confirmed by (1)H NMR and LC/MS. Most recently, a facile work-up of the geometric mixture formed during total synthesis was found to provide multigrams of the targeted all-E geometric isomer of lycophyll. The acquisition of modest quantities of this specific lycopene analog allows its therapeutic potential to be explored.