Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: thermodynamic and functional consequences of structural symmetry.
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Experimental support for the evolution of symmetric protein architecture from a simple peptide motifBacktracking on the folding landscape of the beta-trefoil protein interleukin-1beta?Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic proteinEngineering a Cysteine-Free Form of Human Fibroblast Growth Factor-1 for "Second Generation" Therapeutic ApplicationEmergence of symmetric protein architecture from a simple peptide motif: evolutionary models.Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility.Purification and Refolding of Overexpressed Human Basic Fibroblast Growth Factor in Escherichia coli.In vitro refolding of triosephosphate isomerase from L. donovani.
P2860
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P2860
Redesigning symmetry-related "mini-core" regions of FGF-1 to increase primary structure symmetry: thermodynamic and functional consequences of structural symmetry.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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name
Redesigning symmetry-related " ...... uences of structural symmetry.
@ast
Redesigning symmetry-related " ...... uences of structural symmetry.
@en
type
label
Redesigning symmetry-related " ...... uences of structural symmetry.
@ast
Redesigning symmetry-related " ...... uences of structural symmetry.
@en
prefLabel
Redesigning symmetry-related " ...... uences of structural symmetry.
@ast
Redesigning symmetry-related " ...... uences of structural symmetry.
@en
P2860
P356
P1433
P1476
Redesigning symmetry-related " ...... quences of structural symmetry
@en
P2093
Vikash Kumar Dubey
P2860
P304
P356
10.1110/PS.051494405
P577
2005-08-04T00:00:00Z