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  • 1
    Electronic Resource
    Electronic Resource
    Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) (1976)
    Springer
    European biophysics journal 2 (1976), S. 159-180 
    Details
    ISSN: 1432-1017
    Keywords: Conformational energy calculations ; Protein conformation ; Molecular mechanics ; Proteinase inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Summary The molecular conformation of the basic pancreatic trypsin inhibitor (BPTI) is known in considerable detail from both X-ray studies in single crystals and NMR studies in solution. The NMR experiments showed that the aromatic rings of the phenylalanyl and tyrosyl residues can undergo rapid rotational motions about the Cβ-Cγ bond. The present paper describes a model investigation of the mechanistic aspects of these intramolecular rotational motions. From calculations of the conformational energies for molecular species derived from the X-ray structure by rotations of individual aromatic rings, it was apparent that the rotational motions of the aromatics could only be understood in a flexible structure. Flexibility was simulated by allowing the protein to relax to an energetically favorable conformation for each of the different rotation states of the aromatic rings. It was then of particular interest to investigate how the perturbations caused by different rotation states of the aromatic rings were propagated in the protein structure. It was found that the rotation axes Cβ-Cγ were only slightly affected (Δχ 1≲20°). The most sizeable perturbations are caused by through space interactions with nearby atoms, which move away from the ring center and thus release the steric hindrance opposing the rotational motions. The values for the energy barriers obtained from the energy minimization are of the same order of magnitude as those measured by NMR.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00863707
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  • 2
    Electronic Resource
    Electronic Resource
    Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments (1999)
    Springer
    Journal of biomolecular NMR 15 (1999), S. 181-184 
    Details
    ISSN: 1573-5001
    Keywords: concatenation ; protein NMR ; resonance assignments ; sensitivity enhancement ; TROSY in triple resonance experiments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In experiments with proteins of molecular weights around 100 kDa the implementation of [15N,1H]-TROSY-elements in [15N]-constant-time triple resonance experiments yields sensitivity enhancements of one to two orders of magnitude. An additional gain of 10 to 20% may be obtained with the use of ‘sensitivity enhancement elements’. This paper describes a novel sensitivity enhancement scheme which is based on concatenation of the 13 Cα → 15N magnetization transfer with the ST2-PT element, and which enables proper TROSY selection of the 15N multiplet components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008358030477
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  • 3
    Electronic Resource
    Electronic Resource
    [13c]-Constant-Time [15n,1h]-Trosy-Hnca for Sequential Assignments of Large Proteins (1999)
    Springer
    Journal of biomolecular NMR 14 (1999), S. 85-88 
    Details
    ISSN: 1573-5001
    Keywords: HNCA with 13C constant-time evolution ; protein NMR ; resonance assignments ; spectral resolution ; triple resonance experiments ; TROSY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The greatly improved sensitivity resulting from the use of TROSY during 15N evolution and amide proton acquisition enables the recording of HNCA spectra of large proteins with constant-time 13Cα evolution. In [13C]-ct-[15N,1H]-TROSY-HNCA experiments with a 2H/13C/15N-labeled 110 kDa protein, 7,8-dihydroneopterin aldolase from Staphylococcus aureus, nearly all correlation peaks seen in the [15N,1H]-TROSY-HNCA spectrum were also detected. The improved resolution in the 13C dimension then enabled a significant number of sequential assignments that could not be obtained with [15N,1H]-TROSY-HNCA without [13C]-constant-time period.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008346931993
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  • 4
    Electronic Resource
    Electronic Resource
    Precise vicinal coupling constants3JHNα in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 257-274 
    Details
    ISSN: 1573-5001
    Keywords: Vicinal spin-spin coupling constants ; J-modulated [15N,1H]-COSY ; Nonlinear fit of J-modulation ; Protein conformation ; NMR structure of proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Improved experimental schemes for the recently introduced J-modulated [15N,1H]-correlation experiment for measurements of the homonuclear amide proton-Cα proton vicinal coupling constants.3JHNα, in uniformly15N-labeled proteins are described, and a nonlinear fit procedure is presented for quantitative evaluation of3JHNα. The method was first tested with the N-terminal DNA-binding domain of the 434 repressor (M=7.3 kDa), where at 13 C precise values of3JHNα in the range 2.0–9.5 Hz were obtained for all residues with resolved15N-1H cross peaks. It was then applied to theAntennapedia homeodomain complexed to a synthetic 14-base pair DNA fragment (molecular weight of the complex ∼ 18 kDa). The3JHNα values measured were found to be in excellent agreement with those predicted from the secondary structure of this protein in the complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01875320
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    Paper (German National Licenses)
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