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Excluded volume in the configurational distribution of a strongly‐denatured protein
Author(s) -
Peterscu AndreiJose,
Receveur Veronique,
Calmettes Patrick,
Durand Dominique,
Smith Jeremy C.
Publication year - 1998
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 - 10.1002/pro.5560070616
Subject(s) - radius of gyration , scattering , neutron scattering , chain (unit) , crystallography , guanidine , chemistry , monte carlo method , denaturation (fissile materials) , physics , folding (dsp implementation) , distribution (mathematics) , radius , small angle neutron scattering , statistical physics , nuclear magnetic resonance , mathematics , quantum mechanics , mathematical analysis , statistics , computer security , organic chemistry , computer science , electrical engineering , nuclear chemistry , engineering , polymer
The configurational distribution of phosphoglycerate kinase (PGK) strongly‐denatured in 4M guanidine hydrochloride solution is investigated using small‐angle neutron scattering (SANS) and Monte Carlo computer simulation. It is shown that the experimental scattering profile can be represented by a random flexible chain of spheres of excess scattering density with excluded volume interactions, the best agreement being achieved when partial sphere intersection is allowed. The radius of gyration of the chain increases by a factor of 4 on denaturation, whereas the average length of segments ˜5 residues long increases by only ˜10%, consistent with a picture in which the large expansion on denaturation originates primarily from increased long‐range flexibility of the polypeptide chain. The results provide a description of the chain statistics from which the construction of starting points for simulation studies of folding of the protein can be envisaged.