HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: ps.04875504v1 13/10/2716    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by He, M. M. Articles by Matthews, B. W. Search for Related Content PubMed PubMed Citation Articles by He, M. M. Articles by Matthews, B. W. Social Bookmarking                   What's this?

Alanine-scanning mutagenesis of the -sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on -sheet formation

Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, University of Oregon, Eugene, Oregon 97403-1229, USA

(RECEIVED May 20, 2004; FINAL REVISION July 7, 2004; ACCEPTED July 7, 2004)

In general, -helical conformations in proteins depend in large part on the amino acid residues within the helix and their proximal interactions. For example, an alanine residue has a high propensity to adopt an -helical conformation, whereas that of a glycine residue is low. The sequence preferences for -sheet formation are less obvious. To identify the factors that influence -sheet conformation, a series of scanning polyalanine mutations were made within the strands and associated turns of the -sheet region in T4 lysozyme. For each construct the stability of the folded protein was reduced substantially, consistent with removal of native packing interactions. However, the crystal structures showed that each of the mutants retained the -sheet conformation. These results suggest that the structure of the -sheet region of T4 lysozyme is maintained to a substantial extent by tertiary interactions with the surrounding parts of the protein. Such tertiary interactions may be important in determining the structures of -sheets in general.

Keywords: -sheet; T4 lysozyme; secondary structure; tertiary interactions; alanine mutagenesis

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04875504.

Reprint requests to: Brian W. Matthews, Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, 1229 University of Oregon, Eugene, OR 97403-1229, USA; e-mail: brian{at}uoxray.uoregon.edu; fax: (541) 346-5870.

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. R. Banatao, D. Cascio, C. S. Crowley, M. R. Fleissner, H. L. Tienson, and T. O. Yeates An approach to crystallizing proteins by synthetic symmetrization PNAS, October 31, 2006; 103(44): 16230 - 16235. [Abstract] [Full Text] [PDF]

				M. Sagermann, W. A. Baase, and B. W. Matthews Sequential reorganization of beta-sheet topology by insertion of a single strand Protein Sci., May 1, 2006; 15(5): 1085 - 1092. [Abstract] [Full Text] [PDF]

				R. Simkovsky and J. King An elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin PNAS, March 7, 2006; 103(10): 3575 - 3580. [Abstract] [Full Text] [PDF]