BIOSIS NO: 99241682
      AUTHOR: Warwicker J; Gane P J
CORP. SOURCE: Inst. Food Res., Reading Lab., Whiteknights Rd., Reading RG6 
              6BZ, UK
       TITLE: A model for prion protein dimerisation based on alpha-helical 
              packing.
      SOURCE: Biochemical and Biophysical Research Communications 226(3). 
              777-782.
        DATE: 1996. 
 STANDARD NO: 0006-291X
    LANGUAGE: English
    ABSTRACT: Residues 109-122 of the human prion protein (PrP) are highly 
              conserved across species, and are predicted to be alpha-
              helical in PrP-c, the cellular form. A computational search of 
              the potential for alpha-helical dimerization has been made for 
              residues 109-122. The conformation which consistently scores 
              highest in terms of burying non-polar surface area is a tight 
              association involving alanine, glycine and valine residues. A 
              model of heterodimerisation for PrP-c and PrP-Sc (the 
              misfolded form) is presented in which species barrier 
              mutations would arise from interaction specificities that 
              would follow, at least in part, the same framework as 
              formation of a putative homodimer.
 DESCRIPTORS: RESEARCH ARTICLE; PRION; PRION PROTEIN; DIMERIZATION; ALPHA-
              HELICAL PACKING; SECONDARY STRUCTURE; BIOCHEMISTRY AND 
              BIOPHYSICS
  SUPER TAXA: Microorganisms; Viruses


   BIOSIS NO: 99194770
      AUTHOR: Wetzel R
CORP. SOURCE: 1732 Hamilton Dr., Phoenixville, PA 19460, USA
       TITLE: For protein misassembly, it's the "I" decade.
      SOURCE: Cell 86(5). 699-702.
        DATE: 1996. 
 STANDARD NO: 0092-8674
    LANGUAGE: English
 DESCRIPTORS: JOURNAL ARTICLE; BIOCHEMISTRY AND BIOPHYSICS; PROTEIN; 
              MISASSEMBLY; FOLDING INTERMEDIATES; DISPOSITION; 
              CONFORMATIONAL CHANGE; AMYLOIDOSIS; PRION DISEASES; METABOLIC 
              DISEASE


   BIOSIS NO: 99194705
      AUTHOR: Hornemann S; Glockshuber R
CORP. SOURCE: Inst. Molekularbiol. Biophys., ETH-Hoenggerberg, HPM E12, CH-
              8093 Zuerich, Switzerland
       TITLE: Autonomous and reversible folding of a soluble amino-
              terminally truncated segment of the mouse prion protein.
      SOURCE: Journal of Molecular Biology 261(5). 614-619.
        DATE: 1996. 
 STANDARD NO: 0022-2836
    LANGUAGE: English
    ABSTRACT: Prion diseases are assumed to be caused by the infectious 
              isoform, PrP-Sc, of a single cellular surface protein, PrP-C. 
              PrP-Sc is an insoluble form of PrP-C and is believed to 
              possess a different three-dimensional fold. It may propagate 
              by causing PrP-C to adopt its own infectious conformation by 
              an unknown mechanism. Studies on folding and thermodynamic 
              stability of prion proteins are essential for understanding 
              the processes underlying the conversion from PrP-C to PrP-Sc, 
              but have so far been hampered by the low solubility of prion 
              proteins in the absence of detergents. Here, we show that the 
              amino-terminally truncated segment of mouse PrP comprising 
              residues 121 to 231 is an autonomous folding unit. It consists 
              predominantly of alpha-helical secondary structure and is 
              soluble at high concentrations up to 1 mM in distilled water. 
              PrP(121-231) undergoes a cooperative and completely reversible 
              unfolding/refolding transition in the presence of guanidinium 
              chloride with a free energy of folding of -22 kj/mol at pH 7. 
              The intrinsic stability of segment 121-231 is not in 
              accordance with present models of the structure of PrP-C and 
              PrP-Sc PrP(121-231) may represent the only part of PrP-C with 
              defined three-dimensional structure.
 DESCRIPTORS: RESEARCH ARTICLE; PRION DISEASES; INFECTIOUS ISOFORMS; PROTEIN 
              FOLDING; THERMODYNAMIC STABILITY
  SUPER TAXA: Animals; Chordates; Vertebrates; Nonhuman Vertebrates; 
              Mammals; Nonhuman Mammals; Rodents