Source:http://linkedlifedata.com/resource/pubmed/id/20877851
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
43
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pubmed:dateCreated |
2010-10-27
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pubmed:abstractText |
Here we report the total synthesis of kaliotoxin by 'one pot' native chemical ligation of three synthetic peptides. A racemic mixture of D- and L-kaliotoxin synthetic protein molecules gave crystals in the centrosymmetric space group P1 that diffracted to atomic-resolution (0.95 Å), enabling the X-ray structure of kaliotoxin to be determined by direct methods.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1364-548X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
21
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8174-6
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pubmed:meshHeading |
pubmed-meshheading:20877851-Amino Acid Sequence,
pubmed-meshheading:20877851-Crystallography, X-Ray,
pubmed-meshheading:20877851-Molecular Sequence Data,
pubmed-meshheading:20877851-Peptides,
pubmed-meshheading:20877851-Protein Structure, Tertiary,
pubmed-meshheading:20877851-Scorpion Venoms,
pubmed-meshheading:20877851-Stereoisomerism
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pubmed:year |
2010
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pubmed:articleTitle |
Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography.
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pubmed:affiliation |
Department of Chemistry, Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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