Imperial College London

Professor Molly Stevens

Faculty of EngineeringDepartment of Materials

Professor of Biomedical Materials and Regenerative Medicine
 
 
 
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Contact

 

+44 (0)20 7594 6804m.stevens

 
 
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Location

 

208Royal School of MinesSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Amdursky:2015:10.1002/cphc.201500260,
author = {Amdursky, N and Stevens, MM},
doi = {10.1002/cphc.201500260},
journal = {Chemphyschem},
pages = {2768--2774},
title = {Circular Dichroism of Amino Acids: Following the Structural Formation of Phenylalanine.},
url = {http://dx.doi.org/10.1002/cphc.201500260},
volume = {16},
year = {2015}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Circular dichroism (CD) is frequently used to assess the secondary structure of peptides and proteins, whereas less attention has been given to their building blocks, that is, single amino acids, as they do not possess a secondary structure. Here, we follow the CD signal of amino acids and reveal that several acids exhibit a unique CD pattern as a function of their concentration. Accordingly, we propose an eight-level classification of the CD signal of the various amino acids. Special focus is given to the CD pattern of phenylalanine (Phe), for which we observe the formation of an ultra-narrow CD peak (full width at high maximum of only 5nm). This CD peak can be attributed to the formation of Phe-based chiral structural features. Further support for the formation of an ordered structure is given by using NMR, and the additional self-assembly process of Phe to tubular structures.
AU - Amdursky,N
AU - Stevens,MM
DO - 10.1002/cphc.201500260
EP - 2774
PY - 2015///
SN - 1439-7641
SP - 2768
TI - Circular Dichroism of Amino Acids: Following the Structural Formation of Phenylalanine.
T2 - Chemphyschem
UR - http://dx.doi.org/10.1002/cphc.201500260
UR - http://hdl.handle.net/10044/1/25717
VL - 16
ER -