awgldk
/
wikidata
/
Login
Register
TriplyDB
Wikidata
Browser
Table
SPARQL
Graphs
1
1
Services
1
1
Assets
0
0
Insights
Schema
BETA
Class frequency
Class hierarchy
Q42699500-E151D72C-FF17-4639-ACD3-527407DEB906
Q42699500-E151D72C-FF17-4639-ACD3-527407DEB906
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42699500-E151D72C-FF17-4639-ACD3-527407DEB906
Single molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins.
P2860
Q42699500-E151D72C-FF17-4639-ACD3-527407DEB906
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42699500-E151D72C-FF17-4639-ACD3-527407DEB906
rank
NormalRank
type
BestRank
Statement
wasDerivedFrom
718ba14ea239dcfcafc38f4da3bb3074491683c4
P2860
Salting the charged surface: pH and salt dependence of protein G B1 stability.