Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
 free
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
 free
 free
 
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve
Pubget Overpricing |  
lüll
Protein aggregation processes: In search of the mechanism Frieden CProtein Sci 2007[Nov]; 16 (11): 2334-44Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered-collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and 19F-NMR methods are discussed.|Amyloid/chemistry[MESH]|Animals[MESH]|Humans[MESH]|Light[MESH]|Magnetic Resonance Spectroscopy/methods[MESH]|Models, Statistical[MESH]|Molecular Conformation[MESH]|Peptides/chemistry[MESH]|Polymers/chemistry[MESH]|Protein Binding[MESH]|Protein Structure, Secondary[MESH]|Proteins/*chemistry[MESH]|Scattering, Radiation[MESH]|Spectrometry, Fluorescence/methods[MESH]|Time Factors[MESH] |
