Restricted mobility of the sole tryptophan in membrane-bound melittin.

Abstract:

:In spite of numerous studies, there appears to be no consensus regarding the orientation and aggregation state of membrane-bound melittin. We report here the restricted environment of the sole tryptophan residue in membrane-bound melittin using environment-induced effects on the rates of solvent relaxation. When incorporated into unilamellar vesicles of dioleoyl-sn-glycero-3-phosphocholine (DOPC), melittin exhibits a red edge excitation shift (REES) of 5 nm. In addition, fluorescence polarization of melittin in the membrane shows both excitation and emission wavelength dependence. Taken together, these observations indicate that the tryptophan residue of melittin is located in a motionally restricted region in the membrane.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Chattopadhyay A,Rukmini R

doi

10.1016/0014-5793(93)80415-q

subject

Has Abstract

pub_date

1993-12-13 00:00:00

pages

341-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80415-Q

journal_volume

335

pub_type

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