Protein folding conformational change

The X-ray crystal structure database led us to believe that peptide bonds adopt either the cis or trans conformation in native proteins [22,128]. However, NMR spectroscopy [143], and in a few cases, crystal structure analysis [144], provide encouraging experimental evidence of conformational peptide bond polymorphism of folded proteins. Furthermore, conformational changes in response to ligand binding, crystallization conditions and point mutations at remote sites are frequent. Consequently, the three-dimensional protein structure database contains homologous proteins that have different native conformations for a critical prolyl bond [12]. 

ALLOSTERY AND PROTEIN SUBSTRATE CONFORMATIONAL CHANGE DURING GroEL/GroES-MEDIATED PROTEIN FOLDING... 

Saibil, H. R., A. L. Horwich, and W. A. Fenton. 2001. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Adv. Protein Chem. 59 45-72. 

Keywords Molecular dynamics, pAT. Protein folding, pH-dependent conformational change... 

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