Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local structural analysis.
- DOI
- 10.1016/j.jsb.2022.107910
- Published
- 2022-10-20
- Container
- J Struct Biol
- Publisher
- Not recorded
- Open access
- no
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Cite this work
BibTeX
@article{allodium:10.1016/j.jsb.2022.107910,
title = {Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local structural analysis.},
author = {Unnikrishnan AC and Shanmugam G.},
year = {2022},
journal = {J Struct Biol},
doi = {10.1016/j.jsb.2022.107910},
url = {https://doi.org/10.1016/j.jsb.2022.107910}
}RIS
TY - JOUR TI - Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local structural analysis. AU - Unnikrishnan AC AU - Shanmugam G. PY - 2022 JO - J Struct Biol DO - 10.1016/j.jsb.2022.107910 UR - https://doi.org/10.1016/j.jsb.2022.107910 ER -
APA
AC, U., & G., S. (2022). Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local structural analysis.. J Struct Biol. https://doi.org/10.1016/j.jsb.2022.107910
Source records
- europe-pmc · retrieved 2026-09-25T15:07:42.872Z