Talk:Sandbox Reserved 198

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==Introduction==
==Introduction==
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The synthesis of a fully active semisynthetic RNase A supports the hypothesis that the amino
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The synthesis of a fully active semisynthetic RNase A supports the
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acid sequence of a protein solely dictates the formation of an active enzyme and demonstrates
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hypothesis that the amino acid sequence of a protein solely dictates
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that an enzyme with the catalytic activity and specificity of a naturally produced enzyme can
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the formation of an active enzyme and demonstrates that an enzyme with
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be made in laboratory. Semisynthetic RNase A illustrates that functional enzymes can be produced
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the catalytic activity and specificity of a naturally produced enzyme can
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from merely the individual constituent amino acid residues. Polypeptide synthesis can provide
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be made in laboratory. Semisynthetic RNase A illustrates that functional
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new routes to the study of enzymes through the selective modification of natural proteins to
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enzymes can be produced from merely the individual constituent amino acid
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residues. Polypeptide synthesis can provide new routes to the study of
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enzymes through the selective modification of natural proteins to
assay individual roles of amino acids in folding and catalysis.
assay individual roles of amino acids in folding and catalysis.
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=='''Function'''==
=='''Function'''==
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The structure to function relationship is clearly exhibited by semisynthetic RNase A. In the
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The structure to function relationship is clearly exhibited by semisynthetic
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RNase A protein, the removal of six C terminal residues, leaving <scene name='Sandbox_Reser
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RNase A. In the RNase A protein, the removal of six C terminal residues,
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ved_198/Rnase_1-118/1'>RNase 1-118</scene>, completely halts enzymatic activity (Martin, 1987).
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leaving <scene name='Sandbox_Reserved_198/Rnase_1-118/1'>RNase 1-118</scene>,
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However, a complex of RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</scene>
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completely halts enzymatic activity (Martin, 1987). However, a complex of
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restores enzymatic activity to RNase A. Upon the addition of the synthetic chain, the semisynthetic
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RNase 1-118 with a synthetic polypeptide comprising the <scene name='Talk:Sandbox_Reserved_198/Synthetic_component_114-124/1'>C terminal residues 114-124</scene>
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enzyme adopts a structure that closely resembles that of natural RNase (Martin, 1987). The
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restores enzymatic activity to RNase A. Upon the addition of the synthetic
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restoration of the structure reconstitutes the enzymatic activity of RNase to 98% (Martin, 1987).
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chain, the semisynthetic enzyme adopts a structure that closely resembles
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that of natural RNase (Martin, 1987). The restoration of the structure
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reconstitutes the enzymatic activity of RNase to 98% (Martin, 1987).
=='''Synthetic Method'''==
=='''Synthetic Method'''==
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The RNase 1-118 was prepared by successive digestion of RNase A pepsin and carboxypeptidase A
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The RNase 1-118 was prepared by successive digestion of RNase A pepsin and
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(Doscher, 1983). The synthetic component, RNase 111-124, was prepared by the use of solid-phase
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carboxypeptidase A (Doscher, 1983). The synthetic component, RNase 111-124,
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peptide synthetic mothods, in which the peptide chain was assembled in the stepwise mannar while
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was prepared by the use of solid-phase peptide synthetic mothods, in which
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it was attached at one end to a solid support. The peptide chain was extented by repetitive steps
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the peptide chain was assembled in the stepwise mannar while it was attached
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of deprotection, neutralization and coupling until the desired sequence was obtained (Lin, 1970).
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at one end to a solid support. The peptide chain was extented by repetitive
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It was important that the synthesis proceeds rapidly and in high yields to prevent side reactions
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steps of deprotection, neutralization and coupling until the desired sequence
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or by-products.
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was obtained (Lin, 1970). It was important that the synthesis proceeds rapidly a
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nd in high yields to prevent side reactions or by-products.
'''Related Web-links'''
'''Related Web-links'''
1. Introduction to Ribonuclease A by Raines:
1. Introduction to Ribonuclease A by Raines:
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http://www.uta.edu/faculty/sawasthi/Enzymology-4351-5324/Class%20Syllabus%20Enzymology/ribonucleaseA.pdf
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http://www.uta.edu/faculty/sawasthi/Enzymology-4351-5324/
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Class%20Syllabus%20Enzymology/ribonucleaseA.pdf
2. Solid Phase Synthesis by Merrifield (Nobel Prize Winner):
2. Solid Phase Synthesis by Merrifield (Nobel Prize Winner):
http://nobelprize.org/nobel_prizes/chemistry/laureates/1984/merrifield-lecture.pdf
http://nobelprize.org/nobel_prizes/chemistry/laureates/1984/merrifield-lecture.pdf
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3. Chemical Synthesis of Proteins:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845543/?tool=pmcentrez
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3. Chemical Synthesis of Proteins:http://www.ncbi.nlm.nih.gov/pmc/articles
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/PMC2845543/?tool=pmcentrez
4. Refined Crystal Structure: http://www.ncbi.nlm.nih.gov/pubmed/3680234
4. Refined Crystal Structure: http://www.ncbi.nlm.nih.gov/pubmed/3680234
'''References'''
'''References'''
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Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined Crystal Structure
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Martin, Philip D., Marilynn S. Doscher, and Brian F. P. Edwards. "The Redefined
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of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution." The Journal of Biological Chemistry
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Crystal Structure of a Fully Active Semisynthetic Ribonuclease at 1.8-A Resolution."
 +
The Journal of Biological Chemistry
262.33 (1987): 15930-5938.
262.33 (1987): 15930-5938.
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Marilynn S. Doscher, Philip D. Martin and Brian F.P. Edwards, "Characerization of the Histidine Proton
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Marilynn S. Doscher, Philip D. Martin and Brian F.P. Edwards, "Characerization
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Nuclear Magnetic Resonance of a Semisynthetic Ribonuclease." Biochemistry, 1983,22,4125-4131.
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of the Histidine Proton Nuclear Magnetic Resonance of a Semisynthetic Ribonuclease."
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Biochemistry, 1983,22,4125-4131.
Lin, M. C. (1970) Journal of Biological Chemistry, 245, 6726-6731.
Lin, M. C. (1970) Journal of Biological Chemistry, 245, 6726-6731.
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David J. Boerema, Valentina. A. T., Stephen B. H. Kent, "Total Synthesis by Modern chemical Ligation
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David J. Boerema, Valentina. A. T., Stephen B. H. Kent, "Total Synthesis by
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Methods and High Resolution (1.1-A) X-ray structure of Ribonuclease A. Biopolymers. 2008;90(3):278-86.
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Modern chemical Ligation Methods and High Resolution (1.1-A) X-ray structure
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of Ribonuclease A. Biopolymers. 2008;90(3):278-86.
[[Link title]]
[[Link title]]

Revision as of 02:34, 14 April 2011

This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200.
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