Structural determinants of the rate of protein folding.
To understand the mechanism of protein folding and to assist rational design of fast-folding, non-aggregating and stable artificial enzymes, it is essential to determine the structural parameters which govern the rate constants of folding, kf. It has been found that -logkf is a linear function of the so-called chain topology parameter (CTP) within the range of 10(-1)s(-1)< or = kf < or =10(8)s(-1). The correlation between -logkf and CTP is much improved than using previously published contact order (CO) method. It has been further suggested that short sequence separations may be preferred for the establishment of stable interactions for the design of novel artificial enzymes and the modification of slow-folding proteins with aggregating intermediates.
Nölting
Bengt
B
Prussian Private Institute of Technology at Berlin, Am Schlosspark 30, Berlin D-13187, Germany. nolting@pitb.de
Schälike
Wolfram
W
Hampel
Patrick
P
Grundig
Florian
F
Gantert
Siegfried
S
Sips
Nicole
N
Bandlow
Wolfhard
W
Qi
Phoebe X
PX
D000818:Animals; D015195:Drug Design; D004798:Enzymes; D008956:Models, Chemical; D011328:Prions; D015202:Protein Engineering; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D004798:Enzymes; D011328:Prions; D011506:Proteins