Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2011 Apr 21;108(19):7787–7792. doi: 10.1073/pnas.1019500108

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

PMC Copyright notice

Fig. 1. — Thermodynamics of folding. (A) Cartoon representation of src SH₃ [Protein Data Bank (PDB) code 1SRL]. Sequence and the corresponding location of secondary structures are given below. The numbering starts at position 9. In ref. 34 there is an additional aspartic acid residue at the C terminal. In addition, the sequence in ref. 34 has arginine at the 52nd position whereas our sequence has glutamine. (B) Fraction of molecules in the native state as a function of denaturant concentration. The folded-unfolded transition region is assessed using full width at half-maximum of , which in experiments and simulations for GdmCl is 1.42 M and 1.71 M respectively. Red (green) are the simulation results for GdmCl (urea) and the black dots are experimental results. (C) The dependence of ΔG_NU([C]) on [C] for GdmCl (Left) and urea (Right). In (B) and (C) the denaturant concentration is in molarity.

Inline graphic — Thermodynamics of folding. (A) Cartoon representation of src SH₃ [Protein Data Bank (PDB) code 1SRL]. Sequence and the corresponding location of secondary structures are given below. The numbering starts at position 9. In ref. 34 there is an additional aspartic acid residue at the C terminal. In addition, the sequence in ref. 34 has arginine at the 52nd position whereas our sequence has glutamine. (B) Fraction of molecules in the native state as a function of denaturant concentration. The folded-unfolded transition region is assessed using full width at half-maximum of , which in experiments and simulations for GdmCl is 1.42 M and 1.71 M respectively. Red (green) are the simulation results for GdmCl (urea) and the black dots are experimental results. (C) The dependence of ΔG_NU([C]) on [C] for GdmCl (Left) and urea (Right). In (B) and (C) the denaturant concentration is in molarity.