PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12414713-0	2002	(13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.	Tyrosine	69-77	motilin	Homo sapiens	90-97	
12414713-1	2002	Tyrosine ring dynamics of the gastrointestinal hormone motilin was studied using two independent physical methods: fluorescence polarization anisotropy decay and NMR relaxation.	Tyrosine	0-8	motilin	Homo sapiens	55-62	
12414713-2	2002	Motilin, a 22-residue peptide, was selectively (13)C labeled in the ring epsilon-carbons of the single tyrosine residue.	Tyrosine	103-111	motilin	Homo sapiens	0-7	
12054506-4	2002	Motilin fragments 1-14 in which residues 1 (Phe), 4 (Ile), and 7 (Tyr) were replaced by Ala showed the largest reduction in potency.	Tyrosine	66-69	motilin	Homo sapiens	0-7	
7729365-6	1995	In addition, the interaction of motilin or the derivative motilin (Y7F) -23W (with tyrosine substituted by phenylalanine and with a tryptophan fluorophore added to the C-terminal) with negatively charged phospholipid vesicles (DOPG) was studied.	Tyrosine	83-91	motilin	Homo sapiens	58-65	
1467441-2	1992	Time-resolved fluorescence and CD spectroscopy were used to characterize the structure and dynamics of the peptide hormone motilin with a single tyrosine residue among its 22 amino acids.	Tyrosine	145-153	motilin	Homo sapiens	123-130