PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26139117-5	2016	Melittin analogues that have a proline residue substituted for an alanine, lysine or cysteine have been studied with both model membrane systems and living cells.	Proline	31-38	melittin	Apis mellifera	0-8	
19417147-5	2009	Melittin is synthesized as promelittin, containing a 22 amino acid NH(2)-terminal prodomain rich in the amino acids proline and alanine.	Proline	116-123	melittin	Apis mellifera	0-8	
10961508-0	2000	A Pro --> Ala substitution in melittin affects self-association, membrane binding and pore-formation kinetics due to changes in structural and electrostatic properties Melittin, the main component of bee venom of Apis mellifera, contains a proline at position 14, which is highly conserved in related peptides of various bee venoms.	Proline	243-250	melittin	Apis mellifera	33-41	
10961508-1	2000	To investigate the structural and functional role of Pro14 a melittin analogue was studied where proline is substituted by an alanine residue (P14A).	Proline	97-104	melittin	Apis mellifera	61-69	
10961508-7	2000	The different features of P14A in aggregation, binding and efflux compared to melittin are mainly ascribable directly to structural changes caused by the proline --> alanine substitution.	Proline	154-161	melittin	Apis mellifera	78-86	
10961508-9	2000	It is suggested that the presence of proline in melittin is not only of structural importance but also influences indirectly the electrostatic properties of the native peptide.	Proline	37-44	melittin	Apis mellifera	48-56