Vibrations-determined properties of green fluorescent protein.

Abstract:

: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 beta-sheet barrel with the central alpha-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 beta-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).

journal_name

Biopolymers

journal_title

Biopolymers

authors

Krasnenko V,Tkaczyk AH,Tkaczyk ER,Farkas O,Mauring K

doi

10.1002/bip.20264

subject

Has Abstract

pub_date

2005-06-15 00:00:00

pages

140-6

issue

3

eissn

0006-3525

issn

1097-0282

journal_volume

78

pub_type

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