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
Q42699500-8F9CC996-632F-49F1-BEB6-AF1D5AFA21BC
Q42699500-8F9CC996-632F-49F1-BEB6-AF1D5AFA21BC
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42699500-8F9CC996-632F-49F1-BEB6-AF1D5AFA21BC
Single molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins.
P2860
Q42699500-8F9CC996-632F-49F1-BEB6-AF1D5AFA21BC
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42699500-8F9CC996-632F-49F1-BEB6-AF1D5AFA21BC
rank
NormalRank
type
BestRank
Statement
wasDerivedFrom
718ba14ea239dcfcafc38f4da3bb3074491683c4
P2860
Reversible mechanical unfolding of single ubiquitin molecules.