Imperial College London

ProfessorPaulFreemont

Faculty of MedicineDepartment of Medicine

Chair in Protein Crystallography
 
 
 
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Contact

 

+44 (0)20 7594 5327p.freemont

 
 
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Location

 

259Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{MacDonald:2016:10.1042/BST20160155,
author = {MacDonald, J and Freemont, PS},
doi = {10.1042/BST20160155},
journal = {Biochemical Society Transactions},
pages = {1523--1529},
title = {Computational protein design with backbone plasticity},
url = {http://dx.doi.org/10.1042/BST20160155},
volume = {44},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The computational algorithms used in the design of artificial proteins have become increasingly sophisticated in recent years, producing a series of remarkable successes. The most dramatic of these is the de novo design of artificial enzymes. The majority of these designs have reused naturally occurring protein structures as ‘scaffolds’ onto which novel functionality can be grafted without having to redesign the backbone structure. The incorporation of backbone flexibility into protein design is a much more computationally challenging problem due to the greatly increased search space, but promises to remove the limitations of reusing natural protein scaffolds. In this review, we outline the principles of computational protein design methods and discuss recent efforts to consider backbone plasticity in the design process.
AU - MacDonald,J
AU - Freemont,PS
DO - 10.1042/BST20160155
EP - 1529
PY - 2016///
SN - 1470-8752
SP - 1523
TI - Computational protein design with backbone plasticity
T2 - Biochemical Society Transactions
UR - http://dx.doi.org/10.1042/BST20160155
UR - http://hdl.handle.net/10044/1/39205
VL - 44
ER -