Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13362-6. doi: 10.1073/pnas.0802252105. Epub 2008 Sep 3.

Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift.

Author information

1
School of Applied Physics, Department of Physics, and Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853, USA.

Abstract

A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 A at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.

PMID:
18768811
PMCID:
PMC2533195
DOI:
10.1073/pnas.0802252105
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center