PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21989967-6	2012	Aib-Gly or (D)Pro-Gly sequences stabilize the turn resulting in residual Trp-Trp interaction at high temperatures, but at the same time the beta-structure (cross strand H-bonds) can become less stable due to constraints of the turn, as seen for (D)Pro-Gly.	Tryptophan	73-76	ANIB1	Homo sapiens	0-3	
10679621-1	2000	Linear Aib-based hexapeptides, of the general formula Ac-Toac-(Aib)(n) -Trp-(Aib)(r) -OtBu [T(Aib)(n) Trp], where n + r = 4, and Toac is a nitroxide spin-labeled C(alpha,alpha)-disubstituted glycine, were investigated by steady-state and time-resolved fluorescence measurements in different solvent media.	Tryptophan	72-75	ANIB1	Homo sapiens	7-10	
10679621-1	2000	Linear Aib-based hexapeptides, of the general formula Ac-Toac-(Aib)(n) -Trp-(Aib)(r) -OtBu [T(Aib)(n) Trp], where n + r = 4, and Toac is a nitroxide spin-labeled C(alpha,alpha)-disubstituted glycine, were investigated by steady-state and time-resolved fluorescence measurements in different solvent media.	Tryptophan	72-75	ANIB1	Homo sapiens	63-66	
10679621-1	2000	Linear Aib-based hexapeptides, of the general formula Ac-Toac-(Aib)(n) -Trp-(Aib)(r) -OtBu [T(Aib)(n) Trp], where n + r = 4, and Toac is a nitroxide spin-labeled C(alpha,alpha)-disubstituted glycine, were investigated by steady-state and time-resolved fluorescence measurements in different solvent media.	Tryptophan	72-75	ANIB1	Homo sapiens	63-66	
10679621-1	2000	Linear Aib-based hexapeptides, of the general formula Ac-Toac-(Aib)(n) -Trp-(Aib)(r) -OtBu [T(Aib)(n) Trp], where n + r = 4, and Toac is a nitroxide spin-labeled C(alpha,alpha)-disubstituted glycine, were investigated by steady-state and time-resolved fluorescence measurements in different solvent media.	Tryptophan	72-75	ANIB1	Homo sapiens	63-66	
31226791-10	2019	The resultant analog sequence Ac-Leu-Thr-Phe-Aib-Glu-Tyr-Trp-Gln-Leu-Cba-Aib-Ser-Ala-Ala-NH2 exhibited high-affinity target binding (Mdm2 Kd = 43 nM) and significant alpha-helicity in circular dichroism studies.	Tryptophan	57-60	ANIB1	Homo sapiens	45-48	
31226791-10	2019	The resultant analog sequence Ac-Leu-Thr-Phe-Aib-Glu-Tyr-Trp-Gln-Leu-Cba-Aib-Ser-Ala-Ala-NH2 exhibited high-affinity target binding (Mdm2 Kd = 43 nM) and significant alpha-helicity in circular dichroism studies.	Tryptophan	57-60	ANIB1	Homo sapiens	73-76	
22052779-4	2012	We observed a progressive increase of the quenching effect of the nitroxyl radical on the fluorescence of the N-terminal tryptophan as TOAC replaces the Aib residue at positions 13, 8, and 4, respectively.	Tryptophan	121-131	ANIB1	Homo sapiens	153-156	
21989967-6	2012	Aib-Gly or (D)Pro-Gly sequences stabilize the turn resulting in residual Trp-Trp interaction at high temperatures, but at the same time the beta-structure (cross strand H-bonds) can become less stable due to constraints of the turn, as seen for (D)Pro-Gly.	Tryptophan	77-80	ANIB1	Homo sapiens	0-3