000 01423 a2200397 4500
005 20250515182055.0
264 0 _c20091020
008 200910s 0 0 eng d
022 _a1089-8638
024 7 _a10.1016/j.jmb.2009.07.078
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMishima, Tomonori
245 0 0 _aResidual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation.
_h[electronic resource]
260 _bJournal of molecular biology
_cOct 2009
300 _a1033-43 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAcids
_xpharmacology
650 0 4 _aAmino Acid Sequence
650 0 4 _aAmyloid
_xchemistry
650 0 4 _aHumans
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aImmunoglobulin lambda-Chains
_xchemistry
650 0 4 _aMolecular Sequence Data
650 0 4 _aProtein Folding
_xdrug effects
650 0 4 _aProtein Stability
_xdrug effects
650 0 4 _aProtein Structure, Secondary
_xdrug effects
650 0 4 _aRecombinant Proteins
_xchemistry
650 0 4 _aSequence Homology, Amino Acid
700 1 _aOhkuri, Takatoshi
700 1 _aMonji, Akira
700 1 _aKanemaru, Takaaki
700 1 _aAbe, Yoshito
700 1 _aUeda, Tadashi
773 0 _tJournal of molecular biology
_gvol. 392
_gno. 4
_gp. 1033-43
856 4 0 _uhttps://doi.org/10.1016/j.jmb.2009.07.078
_zAvailable from publisher's website
999 _c19055027
_d19055027