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  • 1
    ISSN: 1432-1424
    Keywords: colicin E1 ; membrane channel ; chemical modification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The two histidine residues of COOH-terminal channel-forming peptides of colicin E1 were modified by addition of a carbethoxy group through pretreatment with diethylpyrocarbonate. The consequences of the modification were examined by the action of the altered product on both phospholipid vesicles and planar membranes. At pH 6, where activity is low, histidine modification resulted in a decrease of the single channel conductance from 20 pS to approximately 9 pS and a decrease in the selectivity for sodium relative to chloride, showing that histidine modification affected the permeability properties of the channel. At pH 4, where activity is high, the single channel conductance and ion selectivity were not significantly altered by histidine modification. The histidine modification assayed at pH 4 resulted in a threefold increase in the rate of Cl− efflux from asolectin vesicles, and a similar increase in conductance assayed with planar membranes. This conductance increase was inferred to arise from an increase in the fraction of bound histidine-modified colicin molecules forming channels at pH 4, since the increase in activity was not due to (i) an increase in binding of the modified peptide, (ii) a change in ion selectivity, (iii) a change of single channel conductance, or (iv) a change in the pH dependence of binding. The sole cysteine in the colicin molecule was modified in 6m urea with 5,5′-dithiobis(2-nitrobenzoic acid). The activities of the colicin and its COOH-terminal tryptic peptide were found to be unaffected by cysteine modification, arguing against a role of (-SH) groups in protein insertion and/or channel formation.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0894
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract  Palaeodata in synthesis form are needed as benchmarks for the Palaeoclimate Modelling Intercomparison Project (PMIP). Advances since the last synthesis of terrestrial palaeodata from the last glacial maximum (LGM) call for a new evaluation, especially of data from the tropics. Here pollen, plant-macrofossil, lake-level, noble gas (from groundwater) and δ18O (from speleothems) data are compiled for 18±2 ka (14C), 32 °N–33 °S. The reliability of the data was evaluated using explicit criteria and some types of data were re-analysed using consistent methods in order to derive a set of mutually consistent palaeoclimate estimates of mean temperature of the coldest month (MTCO), mean annual temperature (MAT), plant available moisture (PAM) and runoff (P-E). Cold-month temperature (MAT) anomalies from plant data range from −1 to −2 K near sea level in Indonesia and the S Pacific, through −6 to −8 K at many high-elevation sites to −8 to −15 K in S China and the SE USA. MAT anomalies from groundwater or speleothems seem more uniform (−4 to −6 K), but the data are as yet sparse; a clear divergence between MAT and cold-month estimates from the same region is seen only in the SE USA, where cold-air advection is expected to have enhanced cooling in winter. Regression of all cold-month anomalies against site elevation yielded an estimated average cooling of −2.5 to −3 K at modern sea level, increasing to ≈−6 K by 3000 m. However, Neotropical sites showed larger than the average sea-level cooling (−5 to −6 K) and a non-significant elevation effect, whereas W and S Pacific sites showed much less sea-level cooling (−1 K) and a stronger elevation effect. These findings support the inference that tropical sea-surface temperatures (SSTs) were lower than the CLIMAP estimates, but they limit the plausible average tropical sea-surface cooling, and they support the existence of CLIMAP-like geographic patterns in SST anomalies. Trends of PAM and lake levels indicate wet LGM conditions in the W USA, and at the highest elevations, with generally dry conditions elsewhere. These results suggest a colder-than-present ocean surface producing a weaker hydrological cycle, more arid continents, and arguably steeper-than-present terrestrial lapse rates. Such linkages are supported by recent observations on freezing-level height and tropical SSTs; moreover, simulations of “greenhouse” and LGM climates point to several possible feedback processes by which low-level temperature anomalies might be amplified aloft.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 2 (1971), S. 289-303 
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Most of the chloroplastb-559 is high potential at neutral pH as defined by hydroquinone reducibility. FCCP* (20 μM) and antimycin A (50 μM) convert high potentialb-559 to a low potential state which can be reduced by ascorbate but not hydroquinone. The low and high potential states of cytochromeb-559 are different forms of the same cytochrome. Three lines of evidence indicate that the cytb-559 oxidized by photosystem I is low potential: (1) theb-559 photooxidized by far-red light in the presence of FCCP (3 μM) is low potentialb-559; (2) the amplitude of theb-559 oxidation by far-red light and the amount of low potentialb-559 present in the dark have the same general dependence on pH; (3) inhibitor studies show that plastoquinone mediates the oxidation of cytb-559 by PS I. The well-known stimulation ofb-559 oxidation by far-red light in the presence of FCCP is attributed to FCCP-facilitated photoconversion of high potentialb-559 to a low potential form. It is concluded that if cytb-559 is oxidized by system I light, then it is a low potential form (E m7≈+80 mV) which is oxidized. It is not proven, however, that a significant amount of cytb-559 is oxidized by PS I under coupled or physiological conditions. Possible thermodynamic regulation of non-cyclic electron flow involving the distribution between high and low potential forms of cytb-559 is discussed.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6881
    Keywords: quinone ; cytochrome b 6 ; cytochrome f ; cytochrome complexes, membrane-bound ; electron transfer ; intraprotein ; iron–sulfur protein ; membranes, energy transduction ; proton translocation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Structural alignment of the integral cytochrome b 6-SU IV subunits with the solved structure of themitochondrial bc 1 complex shows a pronounced asymmetry. There is a much higher homology onthe p-side of the membrane, suggesting a similarity in the mechanisms of intramembrane andinterfacial electron and proton transfer on the p-side, but not necessarily on the n-side. Structuraldifferences between the bc 1 and b 6 f complexes appear to be larger the farther the domain or subunitis removed from the membrane core, with extreme differences between cytochromes c 1 and f. Aspecial role for the dimer may involve electron sharing between the two hemes b p, which is indicatedas a probable event by calculations of relative rate constants for intramonomer heme b p → hemeb n, or intermonomer heme b p → heme b p electron transfer. The long-standing observation offlash-induced oxidation of only ∼0.5 of the chemical content of cyt f may be partly a consequence ofthe statistical population of ISP bound to cyt f on the dimer. It is proposed that the p-side domainof cyt f is positioned with its long axis parallel to the membrane surface in order to: (i) allow itslarge and small domains to carry out the functions of cyt c 1 and suVIII, respectively, of the bc 1complex, and (ii) provide maximum dielectric continuity with the membrane. (iii) This positionwould also allow the internal water chain (“proton wire”) of cyt f to serve as the p-side exit portfor an intramembrane H+ transfer chain that would deprotonate the semiquinol located in themyxothiazol/MOA-stilbene pocket near heme b p. A hypothesis is presented for the identity of theamino acid residues in this chain.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Plant and soil 57 (1980), S. 491-496 
    ISSN: 1573-5036
    Keywords: Aster tripolium ; Compositae ; Heavy metals ; Honey ; Lead ; Pollen ; Taraxacum officinale
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Concentrations of heavy metals in the honey, derived fromAster tripolium was the starting-point for this investigation. Lead content of pollen inAster tripolium andTaraxacum officinale is mainly due to airborne lead. Accumulation of other heavy metals such as zinc and copper in pollen occur mainly via a translocation process from roots to flowers.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Photosynthesis research 10 (1986), S. 393-403 
    ISSN: 1573-5079
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A sumary of biochemical, biophysical, and molecular biological data is presented which led to the identification of two different polypeptides (α and β, MW=9.16 and 4.27 kDa) in the cytochrome b-559 protein. The presence of a single His residue on each polypeptide, and the conclusion from spectroscopy that the heme coordination must be bis-histidine led to an obligatory requirement for coordination of a single heme through a heme cross-linked dimer. This structure does not have a precedent among soluble or membrane bound cytochromes. The possible participation of the cytochrome in the pathway of photoactivation is discussed.
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  • 7
    ISSN: 1573-5079
    Keywords: cytochrome b-559 ; Photosystem II reaction center ; thylakoid membrane ; assembly ; repair cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Stromal membranes enriched in PS I contain a low potential cytochrome with a reduced α-band peak close to 560 nm. The identity of this cytochrome component has been ascribed either to a low potential form of the Photosystem II cytochrome b-559 or to a different cytochrome with a reduced α-band of 560 nm. The half-bandwidth of the 560 nm component in stromal membranes is identical to that of purified cytochrome b-559. Western blots show that the stromal membranes contain an amount of PS II cytochrome b-559 α-subunit that is more than sufficient to account for the cytochrome b-560 detected spectrophotometrically in these membranes. These immunochemical data and the similarity of (i) the spectral peaks, and (ii) the redox properties of low potential PS II cytochrome b-559 and the b-560 component, suggest that the simplest inference is that the cytochrome b-560 protein in stromal membranes is identical to the PS II cytochrome b-559.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Water, air & soil pollution 70 (1993), S. 19-37 
    ISSN: 1573-2932
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract There is great uncertainty with regard to the future role of the terrestrial biosphere in the global carbon cycle. The uncertainty arises from both an inadequate understanding of current pools and fluxes as well as the potential effects of rising atmospheric concentrations of CO2 on natural ecosystems. Despite these limitations, a number of studies have estimated current and future patterns of terrestrial carbon storage. Future estimates focus on the effects of a climate change associated with a doubled atmospheric concentration of CO2. Available models for examining the dynamics of terrestrial carbon storage and the potential role of forest management and landuse practices on carbon conservation and sequestration are discussed.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-6881
    Keywords: Cytochromebc 1 ; electron transfer ; energy transduction ; membrane protein ; structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The following findings concerning the structure of the cytochromeb 6 f complex and its component polypeptides, cytb 6, subunit IV and cytochromef subunit are discussed: (1) Comparison of the amino acid sequences of 13 and 16 cytochromeb 6 and subunit IV polypeptides, respectively, led to (a) reconsideration of the helix lengths and probable interface regions, (b) identification of two likely surface-seeking helices in cytb 6 and one in SU IV, and (c) documentation of a high degree of sequence invariance compared to the mitochondrial cytochrome. The extent of identity is particularly high (88% for conserved and pseudoconserved residues) in the segments of cytb 6 predicted to be extrinsic on then-side of the membrane. (2) The intramembrane attractive forces betweentrans-membrane helices that normally stabilize the packing of integral membrane proteins are relatively weak. (3) The complex isolated in dimeric form has been visualized, along with isolated monomer, by electron microscopy. The isolated dimer is much more active than the monomer, is the major form of the complex isolated and purified from chloroplasts, and is inferred to be a functional form in the membrane. (4) The isolated cytb 6 f complex contains one molecule of chlorophylla. (5) The structure of the 252 residue lumen-side domain of cytochromef isolated from turnip chloroplasts has been solved by X-ray diffraction analysis to a resolution of 2.3 Å.
    Type of Medium: Electronic Resource
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  • 10
    Publication Date: 2016-11-07
    Print ISSN: 0038-6308
    Electronic ISSN: 1572-9672
    Topics: Physics
    Published by Springer
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