1l24

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[[Image:1l24.jpg|left|200px]]
[[Image:1l24.jpg|left|200px]]
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{{Structure
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|PDB= 1l24 |SIZE=350|CAPTION= <scene name='initialview01'>1l24</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1l24", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
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{{STRUCTURE_1l24| PDB=1l24 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l24 OCA], [http://www.ebi.ac.uk/pdbsum/1l24 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l24 RCSB]</span>
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'''ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING'''
'''ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING'''
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Nicholson, H.]]
[[Category: Nicholson, H.]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:27:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:55 2008''
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Revision as of 20:27, 2 May 2008

Template:STRUCTURE 1l24

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING


Overview

It is proposed that the stability of a protein can be increased by selected amino acid substitutions that decrease the configurational entropy of unfolding. Two such substitutions, one of the form Xaa----Pro and the other of the form Gly----Xaa, were constructed in bacteriophage T4 lysozyme at sites consistent with the known three-dimensional structure. Both substitutions stabilize the protein toward reversible and irreversible thermal denaturation at physiological pH. The substitutions have no effect on enzymatic activity. High-resolution crystallographic analysis of the proline-containing mutant protein (Ala-82----Pro) shows that its three-dimensional structure is essentially identical with the wild-type enzyme. The overall structure of the other mutant enzyme (Gly-77----Ala) is also very similar to wild-type lysozyme, although there are localized conformational adjustments in the vicinity of the altered amino acid. The combination of a number of such amino acid replacements, each of which is expected to contribute approximately 1 kcal/mol (1 cal = 4.184 J) to the free energy of folding, may provide a general strategy for substantial improvement in the stability of a protein.

About this Structure

1L24 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding., Matthews BW, Nicholson H, Becktel WJ, Proc Natl Acad Sci U S A. 1987 Oct;84(19):6663-7. PMID:3477797 Page seeded by OCA on Fri May 2 23:27:12 2008

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