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  • Amino acid type classification  (1)
  • Deuteration  (1)
  • Multi-dimensional NMR spectroscopy  (1)
  • Physics  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types (1996)
    Springer
    Journal of biomolecular NMR 8 (1996), S. 360-368 
    Details
    ISSN: 1573-5001
    Keywords: Isotope labelling ; Deuteration ; Resonance assignment ; Global fold ; Larger proteins ; ras p21
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A combination of calculation and experiment is used to demonstrate that the global fold of larger proteins can be rapidly determined using limited NMR data. The approach involves a combination of heteronuclear triple resonance NMR experiments with protonation of selected residue types in an otherwise completely deuterated protein. This method of labelling produces proteins with α-specific deuteration in the protonated residues, and the results suggest that this will improve the sensitivity of experiments involving correlation of side-chain (1H and 13C) and backbone (1H and 15N) amide resonances. It will allow the rapid assignment of backbone resonances with high sensitivity and the determination of a reasonable structural model of a protein based on limited NOE restraints, an application that is of increasing importance as data from the large number of genome sequencing projects accumulates. The method that we propose should also be of utility in extending the use of NMR spectroscopy to determine the structures of larger proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410335
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  • 2
    Electronic Resource
    Electronic Resource
    A1H-15N NM R study of human c-Ha-ras protein: Biosynthetic incorporation of15N-labeled amino acids (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 71-82 
    Details
    ISSN: 1573-5001
    Keywords: Selective15N-labeling ; Ras protein ; Amino acid type classification ; HMQC ; HSQC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A1H-15N NMR study was performed on the GDP-bound form of a truncated human c-Ha-ras oncogene product (171 amino acid residues). Resonance cross peaks of the backbone amide1H-15N nuclei of a uniformly15N-labeled protein were observed with heteronuclear-single-quantum coherence spectroscopy (HSQC). In order to resolve overlapping cross peaks, selective15N-labeling of one or two types of amino acid residues (Ala, Arg, Asx, Glx, Gly, His, lie, Leu, Lys, Met, Phe, Ser; Thr, Tyr and/or Val) was carried out using appropriateE. coli mutant strains. By this procedure, all the backbone1H-15N cross peaks were classified into amino acid types.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02192801
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence-specific 1H and 15N resonance assignments and secondary structure of GDP-bound human c-Ha-Ras protein in solution (1993)
    Springer
    Journal of biomolecular NMR 3 (1993), S. 165-184 
    Details
    ISSN: 1573-5001
    Keywords: GTP binding protein ; Oncogene product ; Multi-dimensional NMR spectroscopy ; Stable isotope labeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary All the backbone 1H and 15N magnetic resonances (except for Pro residues) of the GDP-bound form of a truncated human c-Ha-ras proto-oncogene product (171 amino acid residues, the Ras protein) were assigned by 15N-edited two-dimensional NMR experiments on selectively 15N-labeled Ras proteins in combination with three-dimensional NMR experiments on the uniformly 15N-labeled protein. The sequence-specific assignments were made on the basis of the nuclear Overhauser effect (NOE) connectivities of amide protons with preceding amide and/or Cαprotons. In addition to sequential NOEs, vicinal spin coupling constants for amide protons and Cα protons and deuterium exchange rates of amide protons were used to characterize the secondary structure of the GDP-bound Ras protein; six β strands and five helices were identified and the topology of these elements was determined. The secondary structure of the Ras protein in solution was mainly consistent with that in crystal as determined by X-ray analyses. The deuterium exchange rates of amide protons were examined to elucidate the dynamic properties of the secondary structure elements of the Ras protein in solution. In solution, the β-sheet structure in the Ras protein is rigid, while the second helix (A66-R73) is much more flexible, and the first and fifth helices (S17-124 and V152-L171) are more rigid than other helices. Secondary structure elements at or near the ends of the effector-region loop were found to be much more flexible in solution than in the crystalline state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00178260
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  • 4
    Electronic Resource
    Electronic Resource
    Studies of the polymerization of diallyl compounds. XXV. Gel point in the polymerization of diallyl esters of aromatic dicarboxylic acids (1977)
    New York : Wiley-Blackwell
    Journal of Polymer Science: Polymer Physics Edition 15 (1977), S. 127-136 
    Details
    ISSN: 0098-1273
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Studies on gelation in the radical polymerization of diallyl dicarboxylates have been conducted by Simpson,9,11 Gordon,10 and Oiwa.13 However, the results obtained have not always been consistent and are still far from full elucidations. In this paper, the gel point in the polymerization of diallyl aromatic dicarboxylates, including diallyl phthalate (DAP), diallyl isophthalate (DAI), and diallyl terephthalate (DAT) is experimentally reexamined in detail and discussed according to Gordon's theory; the discrepancy between actual and theoretical gel point conversion was quite large and was enhanced in the order DAT 〉 DAI 〉 DAP. Moreover, from detailed inquiry into the primary chain length of the prepolymer it is suggested that the intramolecular chain transfer reaction plays an important role in the polymerization of diallyl ester accompanying the intramolecular cyclization reaction. The polydispersity coefficient (Pw,0/Pn,0) of the initial prepolymer of DAP is also estimated to be 2.0 from the extrapolation of Pw/Pn to zero conversion.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1977.180150111
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