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
Right arrow Citation Map
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by BRYSON, J. W.
Right arrow Articles by DEGRADO, W. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by BRYSON, J. W.
Right arrow Articles by DEGRADO, W. F.
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 7, Issue 6 1404-1414, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

From coiled coils to small globular proteins: Design of a native-like three-helix bundle

J. W. BRYSON, J. R. DESJARLAIS, T. M. HANDEL and W. F. DEGRADO
The DuPont Merck Pharmaceutical Company, P.O. Box 80400, Wilmington, Delaware Present address: Ecogen Inc., 2000 Cabot Blvd. West, Langhorne, Pennsylvania 19047.

A monomolecular native-like three-helix bundle has been designed in an iterative process, beginning with a peptide that noncooperatively assembled into an antiparallel three-helix bundle. Three versions of the protein were designed in which specific interactions were incrementally added. The hydrodynamic and spectroscopic properties of the proteins were examined by size exclusion chromatography, sedimentation equilibrium, fluorescence spectroscopy, and NMR. The thermodynamics of folding were evaluated by monitoring the thermal and guanidine-induced unfolding transitions using far UV circular dichroism spectroscopy. The attainment of a unique, native-like state was achieved through the introduction of: (1) helix capping interactions; (2) electrostatic interactions between partially exposed charged residues; (3) a diverse collection of apolar side chains within the hydrophobic core.
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?


This article has been cited by other articles:


Home page
 J BiochemHome page
K. Ogata, K. Soejima, and J. Higo
A Monte Carlo Sampling Method of Amino Acid Sequences Adaptable to Given Main-Chain Atoms in the Proteins
J. Biochem., October 1, 2006; 140(4): 543 - 552.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
S. Park, Y. Xu, X. F. Stowell, F. Gai, J. G. Saven, and E. T. Boder
Limitations of yeast surface display in engineering proteins of high thermostability
Protein Eng. Des. Sel., May 1, 2006; 19(5): 211 - 217.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Zhu, D. O. V. Alonso, K. Maki, C.-Y. Huang, S. J. Lahr, V. Daggett, H. Roder, W. F. DeGrado, and F. Gai
Ultrafast folding of {alpha}3D: A de novo designed three-helix bundle protein
PNAS, December 23, 2003; 100(26): 15486 - 15491.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
X. Fu, H. Kono, and J. G. Saven
Probabilistic approach to the design of symmetric protein quaternary structures
Protein Eng. Des. Sel., December 1, 2003; 16(12): 971 - 977.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
C. M. Kraemer-Pecore, J. T.J. Lecomte, and J. R. Desjarlais
A de novo redesign of the WW domain
Protein Sci., October 1, 2003; 12(10): 2194 - 2205.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. M. Ellerby, S. Lee, L. M. Ellerby, S. Chen, T. Kiyota, G. del Rio, G. Sugihara, Y. Sun, D. E. Bredesen, W. Arap, et al.
An Artificially Designed Pore-forming Protein with Anti-tumor Effects
J. Biol. Chem., September 12, 2003; 278(37): 35311 - 35316.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
B. S. Frank, D. Vardar, D. A. Buckley, and C. J. McKnight
The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain
Protein Sci., March 1, 2002; 11(3): 680 - 687.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. L. Wilson, R. Martin, S. Hong, M. Cronin-Golomb, C. A. Mirkin, and D. L. Kaplan
Surface organization and nanopatterning of collagen by dip-pen nanolithography
PNAS, November 9, 2001; (2001) 241323198.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. L. Ogihara, G. Ghirlanda, J. W. Bryson, M. Gingery, W. F. DeGrado, and D. Eisenberg
Design of three-dimensional domain-swapped dimers and fibrous oligomers
PNAS, February 13, 2001; 98(4): 1404 - 1409.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. J. Havranek and P. B. Harbury
Tanford-Kirkwood electrostatics for protein modeling
PNAS, September 28, 1999; 96(20): 11145 - 11150.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. T. R. Walsh, H. Cheng, J. W. Bryson, H. Roder, and W. F. DeGrado
Solution structure and dynamics of a de novo designed three-helix bundle protein
PNAS, May 11, 1999; 96(10): 5486 - 5491.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
P. B. Harbury, J. J. Plecs, B. Tidor, T. Alber, and P. S. Kim
High-Resolution Protein Design with Backbone Freedom
Science, November 20, 1998; 282(5393): 1462 - 1467.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. L. Wilson, R. Martin, S. Hong, M. Cronin-Golomb, C. A. Mirkin, and D. L. Kaplan
Surface organization and nanopatterning of collagen by dip-pen nanolithography
PNAS, November 20, 2001; 98(24): 13660 - 13664.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by The Protein Society.