PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28073045-4	2017	The hydrophobic Bp1 peptide with a cysteine residue adsorbs irreversibly onto Au surfaces due to thiol bond formation, while on hydrophobic CH3 SAM surface, the interactions are hydrophobic in nature.	Cysteine	35-43	BP1	Homo sapiens	16-19	
9405229-2	1997	Kd values for wild-type BP1 and cysteine-modified BP1 were found to be in the range of 60 to 70 nM for both peptides, indicating that free sulfhydryl groups of the cysteines within the peptide are not required for high affinity TAR binding.	Cysteine	32-40	BP1	Homo sapiens	50-53	
9405229-2	1997	Kd values for wild-type BP1 and cysteine-modified BP1 were found to be in the range of 60 to 70 nM for both peptides, indicating that free sulfhydryl groups of the cysteines within the peptide are not required for high affinity TAR binding.	Cysteine	164-173	BP1	Homo sapiens	24-27	
9405229-2	1997	Kd values for wild-type BP1 and cysteine-modified BP1 were found to be in the range of 60 to 70 nM for both peptides, indicating that free sulfhydryl groups of the cysteines within the peptide are not required for high affinity TAR binding.	Cysteine	164-173	BP1	Homo sapiens	50-53