Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by CHEN, L.
Right arrow Articles by PIELAK, G. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by CHEN, L.
Right arrow Articles by PIELAK, G. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 6, Issue 5 1038-1046, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Design, synthesis, expression, and characterization of the genes for mouse Fc{gamma}RIIb1 and Fc{gamma}RIIb2 cytoplasmic regions

L. CHEN, N. L. THOMPSON and G. J. PIELAK
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290

The cytoplasmic regions of the mouse low-affinity Fc{gamma}RII isoforms, mFc{gamma}RIIb1, and mFc{gamma}RIIb2, play a key role in signal transduction by mediating different cellular functions. mFc{gamma}RIIb1 has a 94-residue cytoplasmic region, whereas mFc{gamma}RIIb2 has a 47-residue cytoplasmic region. Genes encoding the cytoplasmic regions of mFc{gamma}RIIb1 (b1-94) and mFc{gamma}RIIb2 (b2-47) were designed, synthesized, and expressed as fusion proteins in Escherichia coli. A sequence-specific protease, thrombin, was used to release the b1-94 peptide, which was purified by using HPLC. The b2-47 peptide was synthesized chemically. CD spectropolarimetry was employed to examine the secondary structures of b1-94 and b2-47. These studies were conducted in aqueous solution, in mixtures of water and trifluoroethanol or methanol, and as a function of temperature. The results indicate that the b1-94 and b2-47 structures are sensitive functions of the solvent environment, and that nonaqueous solvents induce significant {alpha}-helical structure.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Protein Society.