. Author manuscript; available in PMC: 2018 May 1.

Published in final edited form as: J Am Soc Mass Spectrom. 2017 Mar 2;28(5):850–858. doi: 10.1007/s13361-017-1601-7

Table 1.

Comparison of the Fab-1:VEGF Complex higher order structure data obtained from different techniques

		Regions/Residues Identified by Different Methods

Protein	Peptides	FPOP^a	Carboxyl Group^a Footprinting	Native Top-Down MS^b with ECD
	V1-16			A1-H12
	V17-23	Y21
	V57-82	M81
VEGF	V83-101	M94	E93

	HC1-19			E1-G10
	HC20-38	H31,M34	D28
	HC44-65	Y54	E57
	HC77-87	M83
	HC88-98		E89
		Y99-Y103
HC	HC99-127	H107-Y109
	HC225-228			S225-K228
	HC229-231			T229-L231

	LC1-18			D1-S9
	LC19-42	Y32-L33
LC	LC46-61	F50, L54

FPOP and carboxyl-group footprinting[7] data indicate peptides/residues with reduced solvent accessibility and are involved in Fab-1:VEGF interaction.

Native top-down MS with ECD[5] identifies flexible regions excluded from the Fab-1:VEGF binding interface.