Go toArchive
Browse byFacets
Bookbag ( 0 )
'Amino Acid Sequence' in keywords
Results  2 Items
Sorted by   
Publication Year
1988 (1)
1979 (1)
1Author    Helmut Meyer, Hanns-Georg KilianRequires cookie*
 Title    Stained Native Collagen: Interpretation of the Small Angle X-ray Scattering and Electron Microscopic Pictures in Terms of the Primary Structure  
 Abstract    The average axial electron-density distribution of stained collagen fibers derived from X-ray sm all angle pattern, is shown to be substantially related to the projection of the polar amino acid residues onto the axis of the m icrofibril taking into consideration the staggering of neighbouring molecules. In order to arrive ultim ately at a quantitative representation of the experim ental data, an additional periodic fluctuation of the density in necessity of this regular m icrophase structure for an of collagen fibers will be indicated . 
  Reference    Z. Naturforsch. 34c, 13 (1979); received July 24/November 3 1978 
  Published    1979 
  Keywords    Collagen, Amino Acid Sequence, Sm all Angle X-Ray Scattering, Electron M icroscopy 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0013.pdf 
 Identifier    ZNC-1979-34c-0013 
 Volume    34 
2Author    Iwan Bissig, RenéA. Brunisholz, Franz Suter, RichardJ. Cogdell, Herbert ZuberRequires cookie*
 Title    The Complete Amino Acid Sequences of the B 800—850 Antenna Polypeptides from Rhodopseudomonas acidophila strain 7750  
 Abstract    Spectrally pure B 800—850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on What-mann DE-52 ion exchange resin. Two low molecular mass polypeptides (a, ß) have been isolated by organic solvent extraction of the lyophilised B 800—850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degrada-tion. B800—850-a consists of 53 amino acids and is 45.3% and 50.9% homologous to the B 800-850-a antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800—850-ß, 41 amino acids) is 61.0% and 56.1% homolo-gous to the corresponding polypeptides of Rb. sphaeroides and Rb. capsulatus. The molar ratio of the two polypeptides is about 1:1. Both polypeptides show a hydrophilic N-terminal domain, a very hydrophobic central domain and a short C-terminal domain. In both polypeptides the typical His residues, identified in all antenna polypeptides of purple nonsulphur bacteria as possible bacteriochlorophyll binding sites, were found. 
  Reference    Z. Naturforsch. 43c, 77—83 (1988); received October 21 1987 
  Published    1988 
  Keywords    B800—850 Antenna Complex, Light-Harvesting Polypeptide, Purple Nonsulfur Bacterium, Amino Acid Sequence, Rhodopseudomonas acidophila 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0077.pdf 
 Identifier    ZNC-1988-43c-0077 
 Volume    43