Linked Life Data

2196876

Source:http://linkedlifedata.com/resource/pubmed/id/2196876

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-8-21
pubmed:abstractText
A new helical protein was designed and synthesized to alter the sequential connectivity of the 4 helices in human growth hormone and to delete the long surface loop structures. The protein accumulated as an insoluble form in E. coli was solubilized and purified to apparent homogeneity in the presence of 7M urea, and refolded by the aid of 1% n-octyl-beta-D-glucopyranoside. The circular dichroism spectrum was typical of a highly helical protein. The molecular weight estimated by gel permeation chromatography and the red-shift of the fluorescence maximum by urea-induced denaturation suggest that the protein folds into a compact globular form. The new protein obtained, however, was destabilized relative to the original human growth hormone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
170
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-10
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Synthesis of a new helical protein: the effect of secondary structure rearrangement on structure formation.
pubmed:affiliation
Protein Engineering Research Institute, Osaka, Japan.
pubmed:publicationType
Journal Article