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The Biochemical Journal|September 1, 1974
Analysis of the code relating sequence to conformation in globular proteins. Development of a stereochemical alphabet on the basis of intra-residue informationB Robson, R H PainThe Biochemical Journal|September 1, 1974
Analysis of the code relating sequence to conformation in globular proteins. An informational analysis of the role of the residue in determining the conformation of its neighbours in the primary sequenceB Robson, R H PainThe Biochemical Journal|May 1, 1976
The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studiesB Robson, R H PainThe Biochemical Journal|May 1, 1976
The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformationB Robson, R H PainThe Biochemical Journal|September 1, 1974
Analysis of the code relating sequence to conformation in globular proteins. The distribution of residue pairs in turns and kinks in the backbone chainB Robson, R H PainSymposia of the Society for Experimental Biology|January 1, 1987
Temperature and macromolecular structure and functionR H PainEuropean Biophysics Journal : EBJ|January 1, 1991
Molten globule intermediates and protein foldingH Christensen, R H PainBiochemical and Biophysical Research Communications|May 1, 1999
Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibitionB Cigić, R H PainFEBS Letters|May 2, 1994
Tumour necrosis factor is in equilibrium with a trimeric molten globule at low pHR Hlodan, R H PainPageof 17