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Key interactions in the immunoglobulin‐like structure of apo‐neocarzinostatin: Evidence from nuclear magnetic resonance relaxation data and molecular dynamics simulations
Author(s) -
IzadiPruneyre Nadia,
Quiniou Éric,
Blouquit Yves,
Perez Javier,
Minard Philippe,
Desmadril Michel,
Mispelter Joël,
Adjadj Élisabeth
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.12201
Subject(s) - molecular dynamics , antiparallel (mathematics) , chemistry , relaxation (psychology) , chromophore , intermolecular force , chemical physics , intramolecular force , crystallography , biophysics , molecule , computational chemistry , stereochemistry , physics , magnetic field , psychology , social psychology , organic chemistry , quantum mechanics , biology
The three‐dimensional structure of apo‐neocarzinostatin (apo‐NCS, MW: ca.11000, antitumoral chromophore carrier protein) is based on a seven‐stranded antiparallel β‐sandwich, very similar to the immunoglobulin folding domain. We investigated the backbone dynamics of apo‐NCS by 13 C‐NMR relaxation measurements and molecular dynamics simulation. Model‐free parameters determined from the experimental data are compared with a 1.5‐nsec molecular simulation of apo‐NCS in aqueous solution. This comparison provides an accurate description of both local and collective movements within the protein. This analysis enabled us to correlate dynamic processes with key interactions of this β‐protein. Local motions that could be relevant for the intermolecular association with the ligand are also described.