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Vibrations‐determined properties of green fluorescent protein
Author(s) -
Krasnenko Veera,
Tkaczyk Alan H.,
Tkaczyk Eric R.,
Farkas Ödön,
Mauring Koit
Publication year - 2005
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20264
Subject(s) - chemistry , normal mode , gibbs free energy , green fluorescent protein , rigidity (electromagnetism) , eigenvalues and eigenvectors , vibration , molecular dynamics , thermodynamics , physics , computational chemistry , quantum mechanics , biochemistry , gene
The physicochemical characteristics of the green fluorescent protein (GFP), including the thermodynamic properties (entropy, enthalpy, Gibbs' free energy, heat capacity), normal mode vibrations, and atomic fluctuations, were investigated. The Gaussian 03 computational chemistry program was employed for normal mode analysis using the AMBER force field. The thermodynamic parameters and atomic fluctuations were then calculated from the vibrational eigenvalues (frequencies) and eigenvectors. The regions of highest rigidity were shown to be the β‐sheet barrel with the central α‐helix, which bears the chromophore. The most flexible parts of the GFP molecule were the outlying loops that cover the top and bottom of the β‐barrel. This way, the balance between rigidity and flexibility is maintained, which is the optimal relationship for protein stability in terms of Gibbs' free energy. This dual‐schemed structure satisfies the requirements for GFP function. In this sense, the structure of GFP resembles a nanoscale drum: a stiff cylinder with flexible vibrating end(s). © 2005 Wiley Periodicals, Inc. Biopolymers 78: 140–146, 2005 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com