NDLI: The role of an l-leucine residue on the conformations of glycyl-l-leucine oligomers and its N- or C-terminal dependence: infrared absorption and Raman scattering studies

Content Provider	Springer Nature Link
Author	Okabayashi, Hiro Fumi Kanbe, Hide Hiro O’Conr, Charmian J.
Copyright Year	2015
Abstract	The conformations of glycyl-l-leucine oligomers (GnL, residue number n = 3, 4, and 5) in the solid state were found to be similar to that of a polyglycine II (PGII). However, for l-leucyl-glycine oligomers (LGn; n = 3, 4, 5) in the solid state, LG3 and LG4 have already been confirmed to take a reverse-turn structure (LG3-type reverse-turn) while LG5 adopts a PGII-type helix. The present results provide evidence that the conformations of l-leucine-containing glycine oligomers depend strongly upon whether the l-leucine residue is placed in the N- or C-terminal position. For the aqueous G3L and G4L samples, we assumed that reverse-turn structures similar to the type II β-turn, rather than the LG3-type reverse-turn, are stabilized in concentrated solution, probably as the result of aggregation. Models to explain the mechanism of these phenomena are presented.
Starting Page	23
Ending Page	34
Page Count	12
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	45
Issue Number	1
e-ISSN	14321017
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2015-09-18
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Glycyl-l-leucine oligomers LG3-type reverse-turn Helical structure l-leucine N- or C-terminal-dependence Biochemistry Biophysics and Biological Physics Cell Biology Neurobiology Membrane Biology Nanotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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