Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Tcherkasskaya, O.
Right arrow Articles by Ptitsyn, O. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tcherkasskaya, O.
Right arrow Articles by Ptitsyn, O. B.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 12, No. 6, 485-490, June 1999
© 1999 Oxford University Press

Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin

Olga Tcherkasskaya1,2,3 and Oleg B. Ptitsyn1,4

1 Laboratory of Experimental and Computational Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-5677, USA, 2 Institute of Macromolecular Compounds, Russian Academy of Sciences, 199004 St Petersburg and 4 Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

The direct energy transfer technique was modified and applied to probe the relative localization of apomyoglobin A-, G- and H-helixes, which are partly protected from deuterium exchange in the equilibrium molten globule state and in the molten globule-like kinetic intermediate. The non-radiative transfer of tryptophan electronic energy to 3-nitrotyrosine was studied in different conformational states of apomyoglobin (native, molten globule, unfolded) and interpreted in terms of average distances between groups of the protein chain. The experimental data show that the distance between the middle of A-helix and the N-terminus of G-helix as well as the distance between the middle of the A-helix and the C-terminus of the H-helix in the molten globule state are close to those in the native state. This is a strong argument in favor of similarity of the overall architecture of the molten globule and native states.

Keywords: apomyoglobin/direct energy transfer/fluorescence/molten globule

3 To whom correspondence should be addressed, at the first address. E-mail: otcherka{at}lmmb.nci.nih.gov


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
O. Tcherkasskaya, V. E. Bychkova, V. N. Uversky, and A. M. Gronenborn
Multisite Fluorescence in Proteins with Multiple Tryptophan Residues. APOMYOGLOBIN NATURAL VARIANTS AND SITE-DIRECTED MUTANTS
J. Biol. Chem., November 10, 2000; 275(46): 36285 - 36294.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.