Alternative conformations of amyloidogenic proteins govern their behavior.
Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis. In addition, newly available moderate to high resolution structural studies are bringing us closer to understanding the structure of amyloid.
Kelly
J W
JW
Department of Chemistry, Texas A&M University, College Station 77843-3255, USA. kelly@chemvx.tamu.edu
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D017772:Amyloid Neuropathies / Q000235:genetics / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism; D000818:Animals; D006801:Humans; D007147:Immunoglobulin Light Chains / Q000737:chemistry; D008958:Models, Molecular; D009113:Muramidase / Q000235:genetics / Q000378:metabolism; D011228:Prealbumin / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship
D000682:Amyloid; D016229:Amyloid beta-Peptides; D007147:Immunoglobulin Light Chains; D011228:Prealbumin; D009113:Muramidase