1996
DOI: 10.1021/ja961046o
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Film Architecture in Biomolecular Assemblies. Effect of Linker on the Orientation of Genetically Engineered Surface-Bound Proteins

Abstract: This contribution presents strategies for the optimization of supramolecular architecture aimed at controlling the organization of biomolecules at solid surfaces. Myoglobin, modified by site-directed mutagenesis to include a unique cysteine residue, is selectively chemisorbed to self-assembled haloalkylsilylated silica surfaces of varying n-alkyl chain length (n = 2, 3, 8, 11, 15) to yield a series of surface-immobilized recombinant protein assemblies. These supramolecular assemblies are probed using tapping m… Show more

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Cited by 73 publications
(54 citation statements)
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“…The same authors also investigated the effect of the linker length on the orientation of proteins specifically attached through a unique Cys residue. 48 For that purpose they used a genetically engineered myoglobin where the original residue Ala126 was mutated to Cys to introduce a unique thiol group in the protein. The mutated myoglobin was then reacted with self-assembled bromoalkylsilylated silica surfaces employing different linear alkyl chains varying in length.…”
Section: Immobilization Of Thiol-containing Proteinsmentioning
confidence: 99%
“…The same authors also investigated the effect of the linker length on the orientation of proteins specifically attached through a unique Cys residue. 48 For that purpose they used a genetically engineered myoglobin where the original residue Ala126 was mutated to Cys to introduce a unique thiol group in the protein. The mutated myoglobin was then reacted with self-assembled bromoalkylsilylated silica surfaces employing different linear alkyl chains varying in length.…”
Section: Immobilization Of Thiol-containing Proteinsmentioning
confidence: 99%
“…Proteins almost inevitably lose their naturally high activities once immobilized. This loss of bioactivity is widely acknowledged and is thought to result from (i) the denaturation of the three-dimensional protein structure [6][7][8], and (ii) the steric hindrance of antigen-recognition sites [9,10]. Although preventing denaturation of immobilized proteins has potentials to greatly improve immunoassay sensitivity, there are only few researches that have actually looked at both the structure and the activity of immobilized proteins, as well as the relationship between them [11].…”
Section: Introductionmentioning
confidence: 99%
“…Our group and others (Chilkoti et al, 1995;Firestone et al, 1996;Iwakura and Kokubu, 1993;Kallwass et al, 1993;McLean et al, 1993;Persson et al, 1990;Stayton et al, 1992;Vigmond et al, 1994) are addressing the issue of site-directed immobilization of enzymes by employing recombinant DNA techniques to engineer single-cysteine residues into the enzyme structure. Indeed, cysteines can be introduced at a position of choice on an enzyme by genetic engineering methods.…”
Section: Introductionmentioning
confidence: 99%