Literature DB >> 2464850

Protein design, a minimalist approach.

W F DeGrado1, Z R Wasserman, J D Lear.   

Abstract

The question of how the amino acid sequence of a protein specifies its three-dimensional structure remains to be answered. Proteins are so large and complex that it is difficult to discern the features in their sequences that contribute to their structural stability and function. One approach to this problem is de novo design of model proteins, much simpler than their natural counterparts, yet containing sufficient information in their sequences to specify a given function (for example, folding in aqueous solution, folding in membranes, or formation of ion channels). Designed proteins provide simple model systems for understanding protein structure and function.

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Year:  1989        PMID: 2464850     DOI: 10.1126/science.2464850

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  96 in total

1.  A new approach to the design of uniquely folded thermally stable proteins.

Authors:  X Jiang; H Farid; E Pistor; R S Farid
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

2.  Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges.

Authors:  P Barthe; S Rochette; C Vita; C Roumestand
Journal:  Protein Sci       Date:  2000-05       Impact factor: 6.725

3.  Orientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay.

Authors:  F Nicol; S Nir; F C Szoka
Journal:  Biophys J       Date:  1999-04       Impact factor: 4.033

4.  Increasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain.

Authors:  X Jiang; J Kowalski; J W Kelly
Journal:  Protein Sci       Date:  2001-07       Impact factor: 6.725

5.  Interactions of the M2delta segment of the acetylcholine receptor with lipid bilayers: a continuum-solvent model study.

Authors:  Amit Kessel; Turkan Haliloglu; Nir Ben-Tal
Journal:  Biophys J       Date:  2003-12       Impact factor: 4.033

Review 6.  How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles.

Authors:  William F DeGrado; Holly Gratkowski; James D Lear
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

Review 7.  Looking at proteins: representations, folding, packing, and design. Biophysical Society National Lecture, 1992.

Authors:  J S Richardson; D C Richardson; N B Tweedy; K M Gernert; T P Quinn; M H Hecht; B W Erickson; Y Yan; R D McClain; M E Donlan
Journal:  Biophys J       Date:  1992-11       Impact factor: 4.033

Review 8.  Applications of biological pores in nanomedicine, sensing, and nanoelectronics.

Authors:  Sheereen Majd; Erik C Yusko; Yazan N Billeh; Michael X Macrae; Jerry Yang; Michael Mayer
Journal:  Curr Opin Biotechnol       Date:  2010-06-18       Impact factor: 9.740

9.  Designing functional metalloproteins: from structural to catalytic metal sites.

Authors:  Melissa L Zastrow; Vincent L Pecoraro
Journal:  Coord Chem Rev       Date:  2013-09       Impact factor: 22.315

10.  Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.

Authors:  Anna F A Peacock; Olga Iranzo; Vincent L Pecoraro
Journal:  Dalton Trans       Date:  2009-01-16       Impact factor: 4.390

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