PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29168280-5	2018	The N-O bond in the products not only acts as a traceless protecting group for beta-amino acids but also undergoes amide formation with alpha-ketoacids derived from Fmoc-protected alpha-amino acids, thus providing expeditious access to alpha-beta2,2 -dipeptides ready for Fmoc-SPPS.	Amides	115-120	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	242-249	
31006946-2	2019	Glutamic acid sequences often exhibit unusual organization into beta2 -type sheets, where bifurcated H bonds formed between glutamic acid side chains and NH in amide bonds on adjacent beta-strands play a paramount role for stabilizing the molecular assembly.	Amides	160-165	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	64-69	
26590100-3	2016	From library synthesis and further optimization efforts, several structurally diverse reverse amides such as 24c and 24i were found to have excellent human beta3-adrenergic potency and good selectivity over the beta1 and beta2 receptors.	Amides	94-100	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	221-226	
27099990-2	2016	Poly(glutamic acid) at low pH self-assembles after incubation at higher temperature into fibrils composed of antiparallel sheets that are stacked in a beta2-type structure whose amide carbonyls have bifurcated H-bonds involving the side chains from the next sheet.	Amides	178-183	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	151-156	
26362583-1	2015	Poly-L-glutamic acid (PLGA) forms amyloid-like beta2-fibrils with the main spectral component of vibrational amide I" band unusually shifted below 1600 cm(-1).	Amides	109-114	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	47-52	
25144464-2	2014	Aggregation of PLGA chains and formation of amyloid-like fibrils was shown to continue on higher levels of superstructural self-assembly coinciding with the appearance of so-called beta2-sheet conformation manifesting in dramatic redshift of infrared amide I" band below 1600 cm(-1).	Amides	251-256	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	181-186	
24559065-0	2014	Density functional theory based study on cis-trans isomerism of the amide bond in homodimers of beta(2,3)- and beta(3)-substituted homoproline.	Amides	68-73	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	96-104	
20509699-3	2010	The beta(2) fibrils are formed upon heating of aqueous solutions of alpha-helical poly(l-glutamic) acid, which leads to a significant increase of pD (pH) of unbuffered samples and a concomitant precipitation of fibrils with unusual infrared traits: amide I" band being dramatically red-shifted to 1596 cm(-1), and the -COOD stretching band split into two peaks around 1730 and 1719 cm(-1).	Amides	249-254	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	4-10	
23161625-3	2012	Uniquely, they catalyze the hydrolysis of beta(3) - and/or beta(2) -amino acid residues from amides and peptides that are otherwise considered proteolytically stable.	Amides	93-99	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	59-66	
20112354-8	2010	The residues with N-terminal methylated amide and a C-terminal ester bond prefer the conformations beta, beta2, and interestingly, the conformation alpha(L).	Amides	40-45	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	105-110