TY - JOUR
T1 - ISAMBARD
T2 - An open-source computational environment for biomolecular analysis, modelling and design
AU - Wood, Christopher W.
AU - Heal, Jack W.
AU - Thomson, Andrew R.
AU - Bartlett, Gail J.
AU - Ibarra, Amaurys
AU - Brady, R. Leo
AU - Sessions, Richard B.
AU - Woolfson, Derek N.
PY - 2017/6/5
Y1 - 2017/6/5
N2 - Motivation The rational design of biomolecules is becoming a reality. However, further computational tools are needed to facilitate and accelerate this, and to make it accessible to more users. Results Here we introduce ISAMBARD, a tool for structural analysis, model building and rational design of biomolecules. ISAMBARD is open-source, modular, computationally scalable and intuitive to use. These features allow non-experts to explore biomolecular design in silico. ISAMBARD addresses a standing issue in protein design, namely, how to introduce backbone variability in a controlled manner. This is achieved through the generalization of tools for parametric modelling, describing the overall shape of proteins geometrically, and without input from experimentally determined structures. This will allow backbone conformations for entire folds and assemblies not observed in nature to be generated de novo, that is, to access the â € dark matter of protein-fold space'. We anticipate that ISAMBARD will find broad applications in biomolecular design, biotechnology and synthetic biology.
AB - Motivation The rational design of biomolecules is becoming a reality. However, further computational tools are needed to facilitate and accelerate this, and to make it accessible to more users. Results Here we introduce ISAMBARD, a tool for structural analysis, model building and rational design of biomolecules. ISAMBARD is open-source, modular, computationally scalable and intuitive to use. These features allow non-experts to explore biomolecular design in silico. ISAMBARD addresses a standing issue in protein design, namely, how to introduce backbone variability in a controlled manner. This is achieved through the generalization of tools for parametric modelling, describing the overall shape of proteins geometrically, and without input from experimentally determined structures. This will allow backbone conformations for entire folds and assemblies not observed in nature to be generated de novo, that is, to access the â € dark matter of protein-fold space'. We anticipate that ISAMBARD will find broad applications in biomolecular design, biotechnology and synthetic biology.
U2 - 10.1093/bioinformatics/btx352
DO - 10.1093/bioinformatics/btx352
M3 - Article
C2 - 28582565
AN - SCOPUS:85030713173
SN - 1367-4803
VL - 33
SP - 3043
EP - 3050
JO - Bioinformatics
JF - Bioinformatics
IS - 19
ER -