Table 1. Experimentally Characterized IDPs from the LEA Family.

PFAMa	Groupb	Classc	Protein	Species	Secondary Structures and Transitions	Methodsd	Reference
PF00477	1	5	Em	Wheat (Triticum aestivum)	17% β-Sheet, 13% α-helix; 29% α-helix with TFE	CD	McCubbin et al. (1985)
			p11	Pea (Pisum sativum)	Largely unstructured in solution; conformation resistant to heat	CD	Russouw et al. (1997)
			rGmD-19	Soybean (Glycine max)	Highly disordered, 6 to 14% poly (l-Pro)-type structure (PII); 30% α-helix with TFE	DSC, CD	Soulages et al. (2002)
			Mt-Em6	M. truncatula	37% α-helix, 10% β-sheet; increase to 60% α-helix upon drying	FTIR	Boudet et al. (2006)
PF00257	2	1	Dsp16	Craterostigma plantagineum	Largely unstructured with some local residual structural elements; TFE promotes its folding	NMR	Lisse et al. (1996)
		4	Cowpea dehydrin	Vigna unguiculata	Largely unstructured; folded into α-helix with SDS	CD	Ismail et al. (1999)
		3	Cu-COR19	C. unshiu	Largely unstructured; α-helix induced by SDS	CD	Hara et al. (2001)
		2(DHNs)	Cor47	Arabidopsis thaliana	5% α-Helix, 15% PII; 50% α-helix with TFE	CD	Mouillon et al. (2006)
		4	Lti30		0.3% α-Helix, 14% PII; 30% α-helix with TFE
		2	Lti29		0.8% α-Helix, 12% PII; 30% α-helix with TFE
		1	Rab18		12% PII; no α-helix induced with TFE
		2 1	ERD10 ERD14		Largely unstructured; α-helix induced by TFE, no structural changes binding to lipid vesicles	NMR and CD	Kovacs et al. (2008)
		1	K2	Vitis riparia	Highly disordered in the middle Φ-region, transient α-helices in K-regions at both ends	NMR	Hughes and Graether (2011)
		1	DHN1	Maize	Largely unstructured; 9.5% α-helix induced by lipid vesicles or SDS	CD	Koag et al. (2003)
		4	Gm-DHN1	Soybean	27% PII at 12°C, 15% PII at 80°C; TFE and SDS induce only moderate α-helix	DSC and CD	Soulages et al. (2003)
		2	Ts-DHN-1 Ts-DHN-2	T. salsuginea	Both largely unstructured; 31% β-sheet, 18% α-helix for TsDHN-1, and 24% β-sheet, 28% α-helix for TsDHN-2 with lipid vesicles	FTIR and CD	Rahman et al. (2010)
PF02987	3	6	D-7	Typha latifolia	Largely unstructured; 24% β-sheet, 51% α-helix upon fast drying, 45% β-sheet, 40% α-helix upon slow drying	FTIR	Wolkers et al. (2001)
		6	COR15A COR15B	Arabidopsis	Both highly disordered; 65% α-helix (COR15A) and 57% α-helix (COR15B) in the dry state	CD	Thalhammet al. (2010)
		6	LEA7	Arabidopsis	Largely unstructured in solution; 15% β-sheet, 27% α-helix in dry state, α-helix is promoted with lipid vesicles	FTIR and CD	Popova et al. (2011)
		6	LEAM	Pea	Largely unstructured in solution; 50% α-helix with SDS, 70% α-helix with TFE or in dry state	FTIR and CD	Tolleter et al. (2007)
PF03760	4	10	Gm-PM16	Soybean	25% α-helix; 90% α-helix with SDS, TFE or upon drying	FTIR and CD	Shih et al. (2004)
		10	LEA18	Arabidopsis	Largely unstructured; 35% β-sheet, 20% α-helix with negatively charged lipid vesicles	CD	Hundertmark et al. (2011)
PF04927	5	11	Mt-PM25	M. truncatula	Mostly unstructured in solution; increase to 56% α-helix and 25% β-sheet upon drying	FTIR and CD	Boudet et al. (2006); Boucher et al. (2010)
PF03242	5	9	Lj-IDP1	Lotus japonicas	Largely unstructured in solution; 40% α-helix, 15% β-sheet induced by TFE or upon drying	CD, NMR, and FTIR	Haaning et al. (2008)

This is a major but not exhaustive list for the experimentally characterized IDPs of LEA family.

^aProtein family (Pfam) ID.

^bFormer LEA protein groups.

^cNew classification according to Jaspard et al. (2012).

^dCircular dichroism (CD), differential scanning calorimetry (DSC), Fourier transform infrared spectroscopy (FTIR), and nuclear magnetic resonance (NMR).