1l24

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{{STRUCTURE_1l24| PDB=1l24 | SCENE= }}
{{STRUCTURE_1l24| PDB=1l24 | SCENE= }}
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'''ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING'''
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===ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_3477797}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 3477797 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3477797}}
==About this Structure==
==About this Structure==
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Nicholson, H.]]
[[Category: Nicholson, H.]]
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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 Wed Jul 2 11:31:45 2008''

Revision as of 08:31, 2 July 2008

Image:1l24.png

Template:STRUCTURE 1l24

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

Template:ABSTRACT PUBMED 3477797

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

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