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Change in backbone torsion angle distribution on protein folding
Author(s) -
Petrescu AndreiJosé,
Calmettes Patrick,
Durand Dominique,
Receveur Veronique,
Smith Jeremy C.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.6.1129
Subject(s) - ramachandran plot , crystallography , protein folding , scattering , chemistry , globular protein , folding (dsp implementation) , torsion (gastropod) , dihedral angle , denaturation (fissile materials) , guanidine , chemical physics , physics , protein structure , molecular physics , hydrogen bond , optics , molecule , biology , biochemistry , electrical engineering , organic chemistry , nuclear chemistry , engineering , zoology
Understanding protein folding requires the determination of the configurational space accessible to the protein at different stages in folding. Here, computer simulation analysis of small angle neutron scattering results is used to probe the change in the distribution of configurations on strong denaturation of a globular protein, phosphoglycerate kinase, in 4 M guanidine hydrochloride solution. To do this atomic‐detail ensembles of the unfolded protein chain are modeled and their scattering profiles compared with the experiment. The local conformational statistics are found to strongly influence the experimental intensity at scattering vectors between 0.05 and 0.3 Å −1 . Denaturation leads to a reduction in the protein atom‐pair distance distribution function over the ∼3‐15 Å region that is associated with a quantifiable shift in the backbone torsional angle (φ,ψ) distribution toward the β region of the Ramachandran plot.