Table 1.

Summary of peptides and proteins studied, including their sequences, melting temperatures T_m (K), folded populations near room temperature and RMSDs (nm) of representative structures from both experiments and current work, as well as respective representative computational studies by other groups.

Name	Sequence	Experiment		Current work			Refs
		Fold%	T m	Fold%	$T_m^g$	RMSD
AK17a	Ac-(AAKAA)3GY-NMe	30 – 35b		42 ± 5	N.D.h,i		57
Fs	Ac-A5(AARAA)3-NMe	~ 50b	~ 300	45 ± 2	N.D.h,i		58,59
GB1p	GEWTYDDATKTFTVTE	~ 30c	< 273	31 ± 9	N.D.h,i	0.11k	60,61,62 21,63,64 65,66
D47P	GEWTYDPATKTFTVTE	~ 50c	299-311	54 ± 7	300-308	0.12	63
GB1m2	GEWTYNPATGKFTVTE	~ 75c	318-322	79 ± 7	324-332	0.12	64
Trp-cage	NLYIQWLKDGGPSSG RPPPS	~ 70d	~ 315	68 ± 9	~ 324	0.13	63,64,67 21,68,69 70,71,72 73,74
BBA5	Ac-YRVpSYDFSRSDEL AKLLRQHAG-NMe	~ 20e	< 273	27 ± 9	N.D.h,i	0.19	75,76,77
α3D	MGSWAEFKQRLAAIK TRLQALGGSEAELAA FEKEIAAFESELQAY KGKGNPEVEALRKEA AAIRDELQAYRHN		> 363f		N.D.h,j	0.34	78,79

^aNote that as AK17 was used to parameterize the force field, it is not included in the test set.

^bHelical contents measured by CD at 300 K.^48,80

^cMeasured by NMR chemical shifts at 298 K.⁵³

^dEstimated from the melting curve at 300 K measured by NMR.⁵⁴

^eMeasured by CD and uorescence experiments at 293 K for its V3Y/F8W mutant.⁷⁵

^fMeasured by CD at pH 7.0.⁸¹

^gSimulated T_m values were determined by surveying all replicas in the REMD simulations for the one in which the probability of folded states is closest to 50%.

^hNot determined.

ⁱFor AK17, Fs, GB1p and BBA5, T_m values could not be determined because the probability of folded states was lower than 50% for all replicas with temperature above 300 K. Below 300 K, the CG water tends to freeze³¹ and, thus, simulations of protein folding become impossible.

^jIt is still difficult to achieve an equilibrium sampling of a protein of such size (73 a.a.), even through REMD, and, therefore, we were not able to determine T_m for α3D.

^kRMSDs were calculated based on backbone+C_β for GB1p, D47P and GB1m2, backbone (3-19) for Trp-cage, backbone (1-22) for BBA5 and Cα for α3D.