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  • Thermophile  (2)
  • Archaebacteria  (1)
  • Conformational energy calculations  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Conformational energy calculations ; Protein conformation ; Molecular mechanics ; Proteinase inhibitor
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00863707
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  • 2
    Digitale Medien
    Digitale Medien
    Fervidobacterium islandicum sp. nov., a new extremely thermophilic eubacterium belonging to the “Thermotogales” (1990)
    Springer
    Archives of microbiology 154 (1990), S. 105-111 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Eubacterium ; Thermophile ; Evolution ; Fervidobacterium ; Lipids ; Thermotoga
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract An extremely thermophilic anaerobic fermentative eubacterium growing at temperatures between 50 and 80°C (opt.: 65°C) was isolated from an Icelandic hot spring. The cells were Gram-negative motile rods, about 1.8 μm in length, and 0.6 μm in width occurring singly and in pairs. About 50% of the cells formed large spheroids at one end similar to Fervidobacterium nodosum. The new isolate H 21 differed from Fervidobacterium nodosum by a 6 mol % higher GC-content of its DNA (41 mol %), its ability to grow on cellulose, and insignificant DNA homology. The lipids of isolate H 21 were similar to that of members of “Thermotogales”. 16S rRNA sequencing of isolate H 21 and Fervidobacterium nodosum indicated (a) that isolate H 21 represents a new species of the genus Fervidobacterium which we name Fervidobacterium islandicum and (b) that the genus Fervidobacterium belongs to the “Thermotogales” branch.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00423318
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  • 3
    Digitale Medien
    Digitale Medien
    Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C (1986)
    Springer
    Archives of microbiology 144 (1986), S. 324-333 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Evolution ; Eubacteria ; Thermophile ; Anaerobe ; Thermotoga maritima
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract A novel type of bacterium has been isolated from various geothermally heated locales on the sea floor. The organisms are strictly anaerobic, rod-shaped, fermentative, extremely thermophilic and grow between 55 and 90°C with an optimum of around 80°C. Cells show a unique sheath-like structure and monotrichous flagellation. By 16S rRNA sequencing they clearly belong to the eubacteria, although no close relationship to any known group could be detected. The majority of their lipids appear to be unique in structure among the eubacteria. Isolate MSB8 is described as Thermotoga maritima, representing the new genus Thermotoga.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00409880
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  • 4
    Digitale Medien
    Digitale Medien
    Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus (1993)
    Springer
    Archives of microbiology 160 (1993), S. 306-311 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Autotroph ; Archaebacteria ; Aquifex ; Hydrogenobacter ; Thermoproteus ; CO2 fixation ; Reductive citric acid cycle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The autotrophic carbon fixation pathway was studied in the thermophilic hydrogen oxidizing eubacterium Aquifex pyrophilus and in the thermophilic sulfur reducing archaebacterium Thermoproteus neutrophilus. Neither organism contained ribulose-1,5-bisphosphate carboxylase activity suggesting that the Calvin cycle is not operating. Rather, all enzymes of the reductive citric acid cycle were found in A. pyrophilus. In T. neutrophilus ATP citrate lyase activity was detected which has not been achieved so far; this finding corroborates earlier work suggesting the presence of the reductive citric acid cycle in this archaebacterium. The reductive citric acid cycle for autotrophic CO2 fixation now has been documented in the eubacterial branches of the proteobacteria, in green sulfur bacteria, and in the thermophilic Knallgas bacteria as well as in the branch of the sulfur dependent archaebacteria.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00292082
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