Protein folding restraints

All these findings rationalize the results obtained so far with the current approach to restraint-based protein fold prediction, and link theoretical and experimental studies of protein folding with theoretical approaches to structure prediction. This is quite exciting, as the convergent points of view of theorists and experimentalists are beginning to have an impact on practical approaches to predict protein structure. 

L. R. Allen and E. Pad,/. Phys. Condens. Matter, 19, 285211 (2007). Transition States for Protein Folding using Molecular Dynamics and Experimental Restraints. 

Ortiz A R, A Kolinski and J Skolnick 1998. Fold Assembly of Small Proteins Using Monte C Simulations Driven by Restraints Derived from Multiple Sequence Alignments. Jourru Molecular Biology 277 419-446. 

AR Ortiz, A Kolinski, J Skolnick. Fold assembly of small proteins using Monte Carlo simulations driven by restraints derived from multiple sequence alignments. J Mol Biol 277 419-448, 1998. 

ApoSAA, an acute-phase protein, is produced quickly in mice and men in response to a stress (e.g., endotoxin administration, etiocholanolone injection). The apoSAA concentrations rise from less than 1% to more than 25% of the total HDL protein content, depending on the degree of stress (B25, B26). In man, major changes in plasma concentration with disease have been reported, e.g., 100-fold or 1000-fold decreases in concentration with resolution of an acute illness (R18). There are reports that glucose infusion in a normal subject (M22) and in hospital patients (M23) may modify HDL composition and increase plasma apoSAA in HDL and, in vervet monkeys, chair restraint rapidly induces apoSAA production (P3, P5). In cynomolgus monkeys, apoSAA is cleared rapidly from the circulation, more rapidly than apoC-III2 and much more rapidly than apoA-I (B19). 

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