Scaling of folding times with protein size.
Current experimental data show a 9-orders-of-magnitude span in the folding times of proteins. Such a wide range is typically considered a direct consequence of the complexity in structural and sequence patterns of natural proteins. By using a database of 69 proteins and peptides analyzed experimentally, we observe that the folding time scales with the number of residues in the protein. The correlation coefficient is 0.74 or higher, and indicates that it is possible to predict the folding time of a protein with a precision of approximately 1.1 times decades from just its size. A simple thermodynamic analysis of this correlation suggests that the smallest proteins are expected to have very marginal free energy barriers to folding.
Naganathan
Athi N
AN
Department of Chemistry and Biochemistry, and Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland 20742, USA.
Muñoz
Victor
V
D004268:DNA-Binding Proteins / Q000737:chemistry; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014157:Transcription Factors / Q000737:chemistry
D004268:DNA-Binding Proteins; C108466:FSD-1 protein, synthetic; D010455:Peptides; D011506:Proteins; D014157:Transcription Factors; D009113:Muramidase; C030526:tendamistate