SwissSidechain: a molecular and structural database of non-natural sidechains.
Details
Download: BIB_1D528EF3931C.P001.pdf (3657.09 [Ko])
State: Public
Version: author
State: Public
Version: author
Serval ID
serval:BIB_1D528EF3931C
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
SwissSidechain: a molecular and structural database of non-natural sidechains.
Journal
Nucleic Acids Research
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Publication state
Published
Issued date
2013
Peer-reviewed
Oui
Volume
41
Number
D1
Pages
D327-D332
Language
english
Notes
Publication types: Journal Article
Article type changed to Review - Bibliomics - Alexandre Pinault
Article type changed to Review - Bibliomics - Alexandre Pinault
Abstract
Amino acids form the building blocks of all proteins. Naturally occurring amino acids are restricted to a few tens of sidechains, even when considering post-translational modifications and rare amino acids such as selenocysteine and pyrrolysine. However, the potential chemical diversity of amino acid sidechains is nearly infinite. Exploiting this diversity by using non-natural sidechains to expand the building blocks of proteins and peptides has recently found widespread applications in biochemistry, protein engineering and drug design. Despite these applications, there is currently no unified online bioinformatics resource for non-natural sidechains. With the SwissSidechain database (http://www.swisssidechain.ch), we offer a central and curated platform about non-natural sidechains for researchers in biochemistry, medicinal chemistry, protein engineering and molecular modeling. SwissSidechain provides biophysical, structural and molecular data for hundreds of commercially available non-natural amino acid sidechains, both in l- and d-configurations. The database can be easily browsed by sidechain names, families or physico-chemical properties. We also provide plugins to seamlessly insert non-natural sidechains into peptides and proteins using molecular visualization software, as well as topologies and parameters compatible with molecular mechanics software.
Pubmed
Web of science
Open Access
Yes
Create date
14/01/2013 16:02
Last modification date
20/08/2019 12:53