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(Semisynthetic Ribonuclease A)
(Semisynthetic Ribonuclease A)
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== Semisynthetic Ribonuclease A ==
== Semisynthetic Ribonuclease A ==
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--[[User:Michael Slack|Michael Slack]] 19:59, 27 March 2011 (IST)Introduction
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--Introduction
The synthesis of a fully active semisynthetic RNase A supports the hypothesis that the amino acid sequence of a protein solely dictates the formation of an active enzyme and demonstrates that an enzyme with the catalytic activity and specificity of a naturally produced enzyme can be made in laboratory. Semisynthetic RNase A illustrates that functional enzymes can be produced from merely the individual constituent amino acid residues. Polypeptide synthesis can provide new routes to the study of enzymes through the selective modification of natural proteins to assay individual roles of amino acids in folding and catalysis.
The synthesis of a fully active semisynthetic RNase A supports the hypothesis that the amino acid sequence of a protein solely dictates the formation of an active enzyme and demonstrates that an enzyme with the catalytic activity and specificity of a naturally produced enzyme can be made in laboratory. Semisynthetic RNase A illustrates that functional enzymes can be produced from merely the individual constituent amino acid residues. Polypeptide synthesis can provide new routes to the study of enzymes through the selective modification of natural proteins to assay individual roles of amino acids in folding and catalysis.

Revision as of 18:07, 27 March 2011

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Semisynthetic Ribonuclease A

--Introduction The synthesis of a fully active semisynthetic RNase A supports the hypothesis that the amino acid sequence of a protein solely dictates the formation of an active enzyme and demonstrates that an enzyme with the catalytic activity and specificity of a naturally produced enzyme can be made in laboratory. Semisynthetic RNase A illustrates that functional enzymes can be produced from merely the individual constituent amino acid residues. Polypeptide synthesis can provide new routes to the study of enzymes through the selective modification of natural proteins to assay individual roles of amino acids in folding and catalysis.

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