PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19618277-0	2009	Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.	Urea	12-16	lactalbumin alpha	Homo sapiens	69-86	
19618277-4	2009	(15)N R(2) values in some regions of all-Ala alpha-LA show significant exchange broadening which is reduced as the urea concentration is increased.	Urea	115-119	lactalbumin alpha	Homo sapiens	45-53	
19618277-6	2009	Residues in the regions corresponding to the B, D and C-terminal 3(10) helices in native alpha-LA show R(2) values and RDC data consistent with some non-random structural propensities even at high urea concentrations.	Urea	197-201	lactalbumin alpha	Homo sapiens	89-97	
15458242-2	2004	We established that the spin diffusion method shows changes in the secondary structure during the unfolding of the alpha-lactalbumin molten globule by urea.	Urea	151-155	lactalbumin alpha	Homo sapiens	115-132	
15558602-0	2005	Characterization of the denaturation of human alpha-lactalbumin in urea by molecular dynamics simulations.	Urea	67-71	lactalbumin alpha	Homo sapiens	46-63	
15558602-1	2005	Molecular dynamics (MD) simulations were used to characterize the non-cooperative denaturation of the molten globule A-state of human alpha-lactalbumin by urea.	Urea	155-159	lactalbumin alpha	Homo sapiens	134-151	
14657374-3	2003	We use NMR data as restraints in a Monte Carlo sampling procedure to determine the ensemble of structures populated by human alpha-lactalbumin in the presence of increasing concentrations of urea.	Urea	191-195	lactalbumin alpha	Homo sapiens	125-142	
15050830-1	2004	NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix.	Urea	45-49	lactalbumin alpha	Homo sapiens	143-160	
15050830-1	2004	NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix.	Urea	45-49	lactalbumin alpha	Homo sapiens	171-179	
15050830-3	2004	The urea-induced unfolding behavior of [28-111] alpha-LA is similar to that of the four-disulfide form of the protein, except that [28-111] alpha-LA is less stable and has greater cooperativity in the loss of different elements of structure.	Urea	4-8	lactalbumin alpha	Homo sapiens	48-56	
3233312-5	1988	The binding of Cu2+ to alpha-lactalbumin lowers significantly its thermostability and stability towards urea denaturation.	Urea	104-108	lactalbumin alpha	Homo sapiens	23-40	
11118458-2	2001	Under denaturing conditions (urea, guanidine hydrochloride, guanidine thiocyanate, organic solvent or elevated temperature) and in the presence of thiol initiator, alpha-LA denatures by shuffling its four native disulfide bonds and converts to a mixture of fully oxidized scrambled structures.	Urea	29-33	lactalbumin alpha	Homo sapiens	164-172	
7986345-2	1994	Secondary structural changes of the cleaved alpha-lactalbumin, in which the two separated polypeptides were joined by disulfide bridges, were examined in solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride.	Urea	197-201	lactalbumin alpha	Homo sapiens	44-61	
7986345-8	1994	On the other hand, the helical structures of the cleaved alpha-lactalbumin began to be disrupted at low concentrations of guanidine hydrochloride and urea compared with that of the intact protein.	Urea	150-154	lactalbumin alpha	Homo sapiens	57-74	
3233312-6	1988	The stability of Cu2+, Ca2+-alpha-lactalbumin against thermal and urea denaturation is similar to that of the apo protein.	Urea	66-70	lactalbumin alpha	Homo sapiens	28-45	
3370237-1	1988	The measured curves of alpha-lactalbumin denaturation kinetics in the presence of urea are described in terms of a single phase.	Urea	82-86	lactalbumin alpha	Homo sapiens	23-40	
26898857-1	2016	We study the orientation of water and urea molecules and protein amide vibrations at aqueous alpha-lactalbumin and alpha-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation.	Urea	38-42	lactalbumin alpha	Homo sapiens	115-132	
29272129-10	2018	However, urea subverts the Glu-induced intermediate formed by alpha-LA, whereas it only slightly destabilizes in the case of RNase A which has a positive surface charge and could possess charge-charge interactions with Glu.	Urea	9-13	lactalbumin alpha	Homo sapiens	62-70