2hl6

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{{STRUCTURE_2hl6| PDB=2hl6 | SCENE= }}
{{STRUCTURE_2hl6| PDB=2hl6 | SCENE= }}
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'''Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS'''
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===Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS===
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==Overview==
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The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA.
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(as it appears on PubMed at http://www.pubmed.gov), where 17027758 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17027758}}
==About this Structure==
==About this Structure==
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[[Category: Esterase]]
[[Category: Esterase]]
[[Category: Glycosylated]]
[[Category: Glycosylated]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:03:21 2008''

Revision as of 06:03, 29 July 2008

Template:STRUCTURE 2hl6

Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex with CAPS

Template:ABSTRACT PUBMED 17027758

About this Structure

2HL6 is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A., Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C, FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758

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