PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11518539-0	2001	Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.	Hydrogen	34-42	lactalbumin alpha	Homo sapiens	86-103	
23155056-4	2013	The results demonstrate the importance of the N-terminal backbone structure and hydrogen-bonding pattern for the stability of alpha-lactalbumin.	Hydrogen	80-88	lactalbumin alpha	Homo sapiens	126-143	
22715785-6	2012	The strength between caffeic acid and alpha-casein was electrostatic attraction (deltaH < 0, deltaS > 0), and that between beta-casein and alpha-Lactalbumin was hydrogen bonding (deltaH < 0, deltaS < 0).	Hydrogen	167-175	lactalbumin alpha	Homo sapiens	145-162	
18177671-6	2008	Compaction of at least one alpha-helix along its axis mediated by internal hydrogen bonds and stabilized by diffuse tertiary structure interactions appears to be one important molecular event during early folding in barstar, CI2, spectrin R16 domain, Arc repressor, alpha-lactalbumin, IM7, IM9, and spectrin R17 domain.	Hydrogen	75-83	lactalbumin alpha	Homo sapiens	266-283	
15670152-3	2005	In the present study, real-time 1H-NMR spectroscopy showed that the ability of R120G alphaB-crystallin to stabilize the partially folded, molten globule state of alpha-lactalbumin was significantly reduced in comparison with wild-type alphaB-crystallin.	Hydrogen	32-34	lactalbumin alpha	Homo sapiens	162-179	
12860137-2	2003	The 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and 20 degrees C is characterised by broad lines which make direct study by NMR methods difficult; this broadening arises from conformational fluctuations throughout the protein on a millisecond to microsecond timescale.	Hydrogen	8-10	lactalbumin alpha	Homo sapiens	42-59	
12860137-2	2003	The 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and 20 degrees C is characterised by broad lines which make direct study by NMR methods difficult; this broadening arises from conformational fluctuations throughout the protein on a millisecond to microsecond timescale.	Hydrogen	8-10	lactalbumin alpha	Homo sapiens	61-69	
12860137-3	2003	Here, we find that an increase in temperature to 50 degrees C leads to a dramatic sharpening of peaks in the 15N-1H HSQC spectrum of human alpha-LA at pH 2.	Hydrogen	113-115	lactalbumin alpha	Homo sapiens	139-147	
12651130-1	2003	Hydrogen exchange (HX) detected by mass spectrometry (MS) was used to analyze the structure of calcium-free alpha-lactalbumin, a model protein with marginal stability.	Hydrogen	0-8	lactalbumin alpha	Homo sapiens	108-125	
2605208-0	1989	Hydrogen exchange of the tryptophan residues in bovine, goat, guinea pig, and human alpha-lactalbumin.	Hydrogen	0-8	lactalbumin alpha	Homo sapiens	84-101	
10092466-4	1999	In particular, we study the hydrogen protection factors in lysozyme studied in transient experiments by Gladwin and Evans and by Nash and Jonas using equilibrium pressure denaturation and the NMR order parameters measured by Dobson and Kim for the homologous protein alpha-lactalbumin.	Hydrogen	28-36	lactalbumin alpha	Homo sapiens	267-284	
1483454-1	1992	1H-NMR assignments have been defined for the aromatic-ring protons of the bovine, guinea pig and human variants of alpha-lactalbumin.	Hydrogen	0-2	lactalbumin alpha	Homo sapiens	115-132	
11419947-9	2001	Thus, the role of LA is to hold Glc by hydrogen bonding with the O-1 hydroxyl group in the acceptor-binding site on beta4Gal-T1, while the N-acetyl group-binding pocket in beta4Gal-T1 adjusts to maximize the interactions with the Glc molecule.	Hydrogen	39-47	lactalbumin alpha	Homo sapiens	18-20	
9133623-0	1997	Hydrogen-exchange kinetics of reduced alpha-lactalbumin bound to the chaperonin GroEL.	Hydrogen	0-8	lactalbumin alpha	Homo sapiens	38-55	
7473740-0	1995	Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.	Hydrogen	45-53	lactalbumin alpha	Homo sapiens	112-129	
7664062-3	1994	Our results, obtained by molecular-sieve chromatography and hydrogen-exchange measurements, show that apo-alpha-lactalbumin in this molten globule state is not bound to GroEL either in the absence or in the presence of KCl.	Hydrogen	60-68	lactalbumin alpha	Homo sapiens	106-123	
8439536-1	1993	Two-dimensional 1H-NMR spectroscopy has been used to study the acid-denatured molten globule (A-state) of alpha-lactalbumin.	Hydrogen	16-18	lactalbumin alpha	Homo sapiens	106-123	
2000138-5	1991	For alpha-lactalbumin, hydrogen exchange kinetics monitored by NMR proved to be crucial for identifying native-like structural features in the stable molten globule state.	Hydrogen	23-31	lactalbumin alpha	Homo sapiens	4-21	
2605208-1	1989	Hydrogen exchange of the individual tryptophan residues of bovine, goat, guinea pig, and human alpha-lactalbumin has been studied by both ultraviolet and NMR spectra.	Hydrogen	0-8	lactalbumin alpha	Homo sapiens	95-112	
2605208-3	1989	Taking account of the thermal unfolding of each alpha-lactalbumin, the hydrogen exchange rates of the individual tryptophan residues are analyzed.	Hydrogen	71-79	lactalbumin alpha	Homo sapiens	48-65	
33784543-6	2021	Both synchronous and 3D fluorescence analysis suggested that the microenvironment around tryptophan residues had changed, which coincided with the result of molecular docking that tryptophan residue of alpha-lactalbumin contributed significantly to hydrogen bonding.	Hydrogen	249-257	lactalbumin alpha	Homo sapiens	202-219	
6047659-2	1967	The hydrogen ion titration curve of alpha-lactalbumin.	Hydrogen	4-12	lactalbumin alpha	Homo sapiens	36-53