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[[Image:1coa.gif|left|200px]]


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==THE EFFECT OF CAVITY CREATING MUTATIONS IN THE HYDROPHOBIC CORE OF CHYMOTRYPSIN INHIBITOR 2==
The line below this paragraph, containing "STRUCTURE_1coa", creates the "Structure Box" on the page.
<StructureSection load='1coa' size='340' side='right'caption='[[1coa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1coa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1coa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coa OCA], [https://pdbe.org/1coa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1coa RCSB], [https://www.ebi.ac.uk/pdbsum/1coa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1coa ProSAT]</span></td></tr>
{{STRUCTURE_1coa|  PDB=1coa |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/ICI2_HORVU ICI2_HORVU] Inhibits both subtilisin and chymotrypsin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1coa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1coa ConSurf].
<div style="clear:both"></div>


'''THE EFFECT OF CAVITY CREATING MUTATIONS IN THE HYDROPHOBIC CORE OF CHYMOTRYPSIN INHIBITOR 2'''
==See Also==
 
*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Hydrophobic residues in the core of a truncated form of chymotrypsin inhibitor 2 (CI2) have been mutated in order to measure their contribution to the stability of the protein. The free energy of unfolding of wild-type and mutants was measured by both guanidinium chloride-induced denaturation and differential scanning calorimetry. The two methods give results for the changes in free energy on mutation that agree to within 1% or 2%. The average change in the free energy of unfolding (+/- standard deviation) for an Ile--&gt;Val mutation is 1.2 +/- 0.1 kcal mol-1, for a Val--&gt;Ala mutation 3.4 +/- 1.5 kcal mol-1, and for either an Ile--&gt;Ala or a Leu--&gt;Ala mutation 3.6 +/- 0.6 kcal mol-1. This gives an average change in the free energy of unfolding for deleting one methylene group of 1.3 +/- 0.5 kcal mol-1. Two significant correlations were found between the change in the free energy of unfolding between wild-type and mutant, delta delta GU-F, and the environment of the mutated residue in the protein. The first is between delta delta GU-F and the difference in side-chain solvent-accessible area buried between wild-type and mutant (correlation coefficient = 0.81, 10 points). The second and slightly better correlation was found between delta delta GU-F and N, the number of methyl/methylene groups within a 6-A radius of the hydrophobic group deleted (correlation coefficient = 0.84, 10 points). The latter correlation is very similar to that found previously for barnase, suggesting that this relationship is general and applies to the hydrophobic cores of other globular proteins. The combined data for C12 and barnase clearly show a better correlation with N (correlation coefficient = 0.87, 30 points) than with the change in the solvent-accessible surface area (correlation coefficient = 0.82, 30 points). This indicates that the packing density around a particular residue is important in determining the contribution the residue makes to protein stability. In one case, Ile--&gt;Val76, a mutation which deletes the C delta 1 methyl group of a buried side chain, a surprising result was obtained. This mutant was found to be more stable than wild-type by 0.2 +/- 0.1 kcal mol-1. We have solved and analyzed the crystal structure of this mutant and find that there are small movements of side chains in the core, the largest of which, 0.7 A, is a movement of the side chain that has been mutated.(ABSTRACT TRUNCATED AT 400 WORDS)
 
==About this Structure==
1COA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COA OCA].
 
==Reference==
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2., Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR, Biochemistry. 1993 Oct 26;32(42):11259-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8218191 8218191]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Elmasry, N.]]
[[Category: Elmasry N]]
[[Category: Fersht, A R.]]
[[Category: Fersht AR]]
[[Category: Jackson, S E.]]
[[Category: Jackson SE]]
[[Category: Johnson, C M.]]
[[Category: Johnson CM]]
[[Category: Moracci, M.]]
[[Category: Moracci M]]
[[Category: Serine protease inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:56:31 2008''

Latest revision as of 09:44, 7 February 2024

THE EFFECT OF CAVITY CREATING MUTATIONS IN THE HYDROPHOBIC CORE OF CHYMOTRYPSIN INHIBITOR 2THE EFFECT OF CAVITY CREATING MUTATIONS IN THE HYDROPHOBIC CORE OF CHYMOTRYPSIN INHIBITOR 2

Structural highlights

1coa is a 1 chain structure with sequence from Hordeum vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ICI2_HORVU Inhibits both subtilisin and chymotrypsin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1coa, resolution 2.20Å

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