This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2nwd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nwd.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nwd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nwd| PDB=2nwd | SCENE= }}
{{STRUCTURE_2nwd| PDB=2nwd | SCENE= }}
-
'''Structure of chemically synthesized human lysozyme at 1 Angstrom resolution'''
+
===Structure of chemically synthesized human lysozyme at 1 Angstrom resolution===
-
==Overview==
+
<!--
-
In this article, we report the total chemical synthesis of human lysozyme. Lysozyme serves as a widespread model system in various fields of biochemical research, including protein folding, enzyme catalysis, and amyloidogenesis. The 130-aa wild-type polypeptide chain of the human enzyme was assembled from four polypeptide segments by using native chemical ligation in a fully convergent fashion. Key to the assembly strategy is the application of the recently developed kinetically controlled ligation methodology, which provides efficient control over the ligation of two peptide (alpha)thioesters to yield a unique product. This result enables the facile preparation of a 64-residue peptide (alpha)thioester; this segment is joined by native chemical ligation to a 66-aa Cys peptide, to yield the target 130-aa polypeptide chain. The synthetic polypeptide chain was folded in vitro into a defined tertiary structure with concomitant formation of four disulfides, as shown by 2D TOCSY NMR spectroscopy. The structure of the synthetic human lysozyme was confirmed by high-resolution x-ray diffraction, giving the highest-resolution structure (1.04 A) observed to date for this enzyme. Synthetic lysozyme was obtained in good yield and excellent purity and had full enzymatic activity. This facile and efficient convergent synthesis scheme will enable preparation of unique chemical analogs of the lysozyme molecule and will prove useful in numerous areas of lysozyme research in the future.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17360367}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17360367 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17360367}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Convergent synthesis]]
[[Category: Convergent synthesis]]
[[Category: Native chemical ligation]]
[[Category: Native chemical ligation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:59:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:41:34 2008''

Revision as of 17:41, 28 July 2008

Image:2nwd.png

Template:STRUCTURE 2nwd

Structure of chemically synthesized human lysozyme at 1 Angstrom resolution

Template:ABSTRACT PUBMED 17360367

About this Structure

2NWD is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Convergent chemical synthesis and high-resolution x-ray structure of human lysozyme., Durek T, Torbeev VY, Kent SB, Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):4846-51. Epub 2007 Mar 8. PMID:17360367

Page seeded by OCA on Mon Jul 28 20:41:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nwd"
Personal tools