Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings

scientific article published on September 2009

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings is …
instance of (P31):
scholarly articleQ13442814
review articleQ7318358

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P356DOI10.1016/J.STR.2009.08.001
P698PubMed publication ID19748338
P5875ResearchGate publication ID26806569

P50authorMalene Ringkjøbing JensenQ24185684
Markus ZweckstetterQ28320715
Sebastian MeierQ43410284
Stephan GrzesiekQ44958017
Martin BlackledgeQ21994149
P2093author name stringChristian Griesinger
Phineus R L Markwick
Pau Bernadó
P2860cites work1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effectsQ29616506
P433issue9
P921main subjectprotein foldingQ847556
P304page(s)1169-1185
P577publication date2009-09-01
P1433published inStructureQ15709970
P1476titleQuantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
P478volume17

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