dc.contributor.author |
Okabayashi, Hiro-Fumi |
|
dc.contributor.author |
Kanbe, Hide-Hiro |
|
dc.contributor.author |
O'Connor, Charmian J |
|
dc.coverage.spatial |
Germany |
|
dc.date.accessioned |
2022-08-22T01:46:28Z |
|
dc.date.available |
2022-08-22T01:46:28Z |
|
dc.date.issued |
2016-01 |
|
dc.identifier.citation |
(2016). European Biophysics Journal, 45(1), 23-34. |
|
dc.identifier.issn |
0175-7571 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/60875 |
|
dc.description.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. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
Springer Nature |
|
dc.relation.ispartofseries |
European biophysics journal : EBJ |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Leucine |
|
dc.subject |
Glycine |
|
dc.subject |
Oligopeptides |
|
dc.subject |
Spectrum Analysis, Raman |
|
dc.subject |
Infrared Rays |
|
dc.subject |
Absorption, Radiation |
|
dc.subject |
Glycyl-L-leucine oligomers |
|
dc.subject |
Helical structure |
|
dc.subject |
L-leucine |
|
dc.subject |
LG3-type reverse-turn |
|
dc.subject |
N- or C-terminal-dependence |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biophysics |
|
dc.subject |
VIBRATIONAL ANALYSIS |
|
dc.subject |
AGGREGATIONAL BEHAVIOR |
|
dc.subject |
MOLECULAR-STRUCTURE |
|
dc.subject |
POLYPEPTIDE-CHAINS |
|
dc.subject |
CRYSTAL-STRUCTURE |
|
dc.subject |
AQUEOUS-SOLUTION |
|
dc.subject |
BETA-TURNS |
|
dc.subject |
PROTEINS |
|
dc.subject |
PEPTIDES |
|
dc.subject |
SPECTRA |
|
dc.subject |
0306 Physical Chemistry (incl. Structural) |
|
dc.subject |
0202 Atomic, Molecular, Nuclear, Particle and Plasma Physics |
|
dc.subject |
0299 Other Physical Sciences |
|
dc.subject |
0601 Biochemistry and Cell Biology |
|
dc.title |
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. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1007/s00249-015-1072-3 |
|
pubs.issue |
1 |
|
pubs.begin-page |
23 |
|
pubs.volume |
45 |
|
dc.date.updated |
2022-07-21T12:57:10Z |
|
dc.rights.holder |
Copyright: The authors |
en |
dc.identifier.pmid |
26385704 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/26385704 |
|
pubs.end-page |
34 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Journal Article |
|
pubs.elements-id |
516763 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Chemistry |
|
dc.identifier.eissn |
1432-1017 |
|
dc.identifier.pii |
10.1007/s00249-015-1072-3 |
|
pubs.record-created-at-source-date |
2022-07-22 |
|
pubs.online-publication-date |
2016-01 |
|