Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides.

Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Research Abstract Details 

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Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Abstract Text:

E J Cantor,E D Atkins,S J Cooper,M J Fournier,T L Mason,D A Tirrell,

The fidelity of bacterial protein synthesis allows the production of architecturally well-defined polymeric materials through precise control of chain length, sequence, stereochemistry, and interchain interactions. In the present paper, we examine the relation between amino acid residue volume and crystalline unit cell dimensions, in a set of periodic protein polymers of repeating unit sequence -(AlaGly)3-X-Gly-, where X is Asn, Phe, Ser, Val, or Tyr. The proteins were overexpressed in Escherichia coli, purified by simple procedures based on acid/ethanol precipitation or insolubility in aqueous sodium dodecyl sulfate, and processed to form oriented crystalline mats by precipitation from formic acid under mechanical shear. X-ray diffraction analyses revealed that the basic structures of the -(AlaGly)3-X-Gly- polymers are identical to that previously reported for [(AlaGly)3-GluGly]36, [Krejchi, M.T., Atkins, E.D.T., Waddon, A.J., Fournier, M.J., Mason, T.L., and Tirrell, D.A. (1994) Science 265, 1427-1432], with the oligoalanylglycine segments forming antiparallel beta-sheets and the substituted amino acids occurring within three-residue folds at the lamellar surfaces. The X-ray diffraction signals for each member of the family index on an orthorhombic unit cell; the a-axis (hydrogen bond direction) and c-axis (chain direction) spacings remain invariant but the b-axis (sheet stacking direction) spacing increases with increasing volume of the substituted amino acid. The results obtained from a variant with alternating Glu and Lys substitution at the X position, together with the results previously reported for poly(L-alanylglycine) [Panitch, A., Matsuki, K., Cantor, E.J., Cooper, S.J., Atkins, E.D.T., Fournier, M.J., Mason, T.L., and Tirrell, D.A. (1997) Macromolecules 30, 42-49] are included for comparison. The average intersheet stacking distance (b/2) increases linearly with the volume of the amino acid inserted at position X. Because the chain-folded lamellar architecture adopted by these periodic polypeptides accommodates a wide range of residues differing in charge, steric bulk, and hydrophobicity, these results illustrate a new approach to the engineering of intermolecular interactions in polymeric solids.

Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Publishing Authors By Initials

EJ Cantor,ED Atkins,SJ Cooper,MJ Fournier,TL Mason,DA Tirrell,

For similar investigative techniques: genetic techniques: genetic engineering: protein engineering research abstracts see: investigative techniques: genetic techniques: genetic engineering: protein engineering research

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Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of biochemistry

VOLUME: 122

Page Numbers: 217-25

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1997

Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Keywords Mesh Terms:

KEYWORDS: Protein Engineering

MESH TERMS: genetics

Chemical & Substance for Abstract: Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. Information

Substance Name: Peptides

Registry Number: 0

Grant and Affiliation Information for Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides.

AFFILIATION: Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003, USA.

Country: JAPAN

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MEDLINETA: J Biochem

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