1rfp: Difference between revisions

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

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

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~~'''~~ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS~~'''~~

===ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS===

~~==Overview==~~

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~~In the N~~-~~terminal region of the alpha~~-~~helix of~~ the ~~c-type lysozymes, two Asx residues exist at~~ the ~~18th and 27th positions. Hen lysozyme has Asp18/Asn27~~ (~~18D/27N), and we prepared three mutant lysozymes, Asn18~~/~~Asn27 (18N~~/~~27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D)~~. ~~The stability of the wild-type (18D/27N~~) ~~lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the alpha-helix~~, ~~while the stability of~~ the ~~18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues~~. ~~Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B~~-~~helix in 18D/27D lysozyme through hydrogen bonding and charge~~-~~helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9354379}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9354379 is the PubMed ID number.

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==About this Structure==

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[[Category: Hydrolase]]

[[Category: Stability]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 07~~:26:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:30:02 2008''

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-[[Image:1rfp.jpg|left|200px]]
+{{Seed}}
+[[Image:1rfp.png|left|200px]]
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 {{STRUCTURE_1rfp|  PDB=1rfp  |  SCENE=  }}
-'''ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS'''
+===ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS===
-==Overview==
+<!--
-In the N-terminal region of the alpha-helix of the c-type lysozymes, two Asx residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27 (18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type (18D/27N) lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the alpha-helix, while the stability of the 18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B-helix in 18D/27D lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_9354379}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9354379 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9354379}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Hydrolase]]
 [[Category: Stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:26:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:30:02 2008''