Detailed Information on Publication Record
2015
HotSpot Wizard 2.0
ŠTOURAČ, Jan, Jaroslav BENDL, Eva ŠEBESTOVÁ, Ondřej VÁVRA, Miloš MUSIL et. al.Basic information
Original name
HotSpot Wizard 2.0
Authors
ŠTOURAČ, Jan (203 Czech Republic, belonging to the institution), Jaroslav BENDL (203 Czech Republic, belonging to the institution), Eva ŠEBESTOVÁ (203 Czech Republic, belonging to the institution), Ondřej VÁVRA (203 Czech Republic, belonging to the institution), Miloš MUSIL (203 Czech Republic, belonging to the institution), Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)
Edition
2015
Other information
Language
English
Type of outcome
Software
Field of Study
10201 Computer sciences, information science, bioinformatics
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
RIV identification code
RIV/00216224:14310/15:00080424
Organization unit
Faculty of Science
Keywords (in Czech)
proteinové inženýrství, design chytrých knihoven, výpočetní mutageneze, predikce hotspotů
Keywords in English
protein engineering; smart library design; computational mutagenesis; hotspot prediction
Technical parameters
Integrated platform for protein engineering.
Tags
Změněno: 23/5/2016 14:10, Ing. Jaroslav Bendl
Abstract
V originále
HotSpot Wizard is a web server for automatic identification of hot spots for engineering of substrate specificity, activity or entantioselectivity of enzymes and for annotation of protein structures. HSW 2.0 integrates 3 databases and 18 computational tools, including our in-house tool for analysis of protein tunnels and channels Caver 3.0. In the output, users can explore hot spots based on 4 protein engineering strategies: (i) functional hot spots represented by highly mutable residues located in the active site pocket or access tunnels, (ii) stability hot spots represented by flexible residues, (iii) stability hot spots identified by back-to-consensus approach, and (iv) correlated hot spots represented by pairs of coevolving residues that modulate enzyme activity and selectivity.
Links
| TA04021380, research and development project |
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