Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
A New Method for Modeling Large-Scale Rearrangements of Protein Domains
 

Summary: A New Method for Modeling Large-Scale
Rearrangements of Protein Domains
Vladimir Maiorov and Ruben Abagyan*
The Skirball Institute of Biomolecular Medicine and Biochemistry Department, New York University Medical Center,
New York, New York
ABSTRACT A method for modeling large-
scale rearrangements of protein domains con-
nected by a single- or a double-stranded linker
is proposed. Multidomain proteins may undergo
substantial domain displacements, while their
intradomain structure remains essentially un-
changed. The method allows automatic identi-
fication of an interdomain linker and builds an
all-atom model of a protein structure in inter-
nal coordinates. Torsion angles belonging to the
interdomain linkers and side chains potentially
able to form domain interfaces are set free
while all remaining torsions, bond lengths, and
bond angles are fixed. Large-scale sampling of
the reduced torsion conformational subspace

  

Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego

 

Collections: Biology and Medicine