1l31: Difference between revisions

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[[Image:1l31.~~jpg~~|left|200px]]

[[Image:1l31.png|left|200px]]

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~~'''~~REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY~~'''~~

===REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY===

~~==Overview==~~

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~~To investigate the relation between protein stability and the predicted stabilities of individual secondary structural elements~~, residue Pro86 in an alpha-helix in phage T4 lysozyme was replaced by ten different amino acids. The x-ray crystal structures of seven of the mutant lysozymes were determined at high resolution. In each case, ~~replacement of~~ the ~~proline resulted in~~ the ~~formation of an extended alpha-helix~~. ~~This involves a large conformational change in residues 81 to 83 and smaller shifts that extend 20 angstroms across the protein surface~~. ~~Unexpectedly~~, ~~all ten amino acid substitutions marginally reduce protein thermostability. This insensitivity of stability to~~ the amino acid at position 86 is not simply explained by statistical and thermodynamic criteria for helical propensity. The observed conformational changes illustrate a general mechanism by which proteins can tolerate mutations.

The line below this paragraph, {{ABSTRACT_PUBMED_3277275}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 3277275 is the PubMed ID number.

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==About this Structure==

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[[Category: Dao-Pin, S.]]

[[Category: Matthews, B W.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:29:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:35:22 2008''

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-[[Image:1l31.jpg|left|200px]]
+{{Seed}}
+[[Image:1l31.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1l31|  PDB=1l31  |  SCENE=  }}
-'''REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY'''
+===REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY===
-==Overview==
+<!--
-To investigate the relation between protein stability and the predicted stabilities of individual secondary structural elements, residue Pro86 in an alpha-helix in phage T4 lysozyme was replaced by ten different amino acids. The x-ray crystal structures of seven of the mutant lysozymes were determined at high resolution. In each case, replacement of the proline resulted in the formation of an extended alpha-helix. This involves a large conformational change in residues 81 to 83 and smaller shifts that extend 20 angstroms across the protein surface. Unexpectedly, all ten amino acid substitutions marginally reduce protein thermostability. This insensitivity of stability to the amino acid at position 86 is not simply explained by statistical and thermodynamic criteria for helical propensity. The observed conformational changes illustrate a general mechanism by which proteins can tolerate mutations.
+The line below this paragraph, {{ABSTRACT_PUBMED_3277275}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3277275 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3277275}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Dao-Pin, S.]]
 [[Category: Matthews, B W.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:29:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:35:22 2008''