Imperial College London
Portrait Picture

Professor Jerry Heng

Faculty of Engineering, Department of Chemical Engineering

Professor in Particle Technology
 
 
 
//

Contact

 

+44 (0)20 7594 0784jerry.heng

 
 
//

Location

 

208ACE ExtensionSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Guo:2021:10.1021/acs.jpclett.1c01622,
author = {Guo, M and Rosbottom, I and Zhou, L and Yong, CW and Zhou, L and Yin, Q and Todorov, IT and Errington, E and Heng, JYY},
doi = {10.1021/acs.jpclett.1c01622},
journal = {Journal of Physical Chemistry Letters},
pages = {8416--8422},
title = {Triglycine (GGG) adopts a polyproline II (pPII) conformation in its hydrated crystal form: revealing the role of water in peptide crystallization},
url = {http://dx.doi.org/10.1021/acs.jpclett.1c01622},
volume = {12},
year = {2021}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Polyproline II (pPII) is a left-handed 31-helix conformation, which has been observed to be the most abundant secondary structure in unfolded peptides and proteins compared to α-helix and β-sheet. Although pPII has been reported as the most stable conformation for several unfolded short chain peptides in aqueous solution, it is rarely observed in their solid state. Here, we show for the first time a glycine homopeptide (gly-gly-gly) adopting the pPII conformation in its crystalline dihydrate structure. The single crystal X-ray structure with molecular dynamic simulation suggests that a network of water and the charged carboxylate group is critical in stabilizing the pPII conformation in solid state, offering an insight into the structures of unfolded regions of proteins and the role of water in peptide crystallization.
AU  - Guo,M
AU  - Rosbottom,I
AU  - Zhou,L
AU  - Yong,CW
AU  - Zhou,L
AU  - Yin,Q
AU  - Todorov,IT
AU  - Errington,E
AU  - Heng,JYY
DO  - 10.1021/acs.jpclett.1c01622
EP  - 8422
PY  - 2021///
SN  - 1948-7185
SP  - 8416
TI  - Triglycine (GGG) adopts a polyproline II (pPII) conformation in its hydrated crystal form: revealing the role of water in peptide crystallization
T2  - Journal of Physical Chemistry Letters
UR  - http://dx.doi.org/10.1021/acs.jpclett.1c01622
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000693398700035&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://pubs.acs.org/doi/10.1021/acs.jpclett.1c01622
UR  - http://hdl.handle.net/10044/1/91822
VL  - 12
ER  -
Download