|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
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|
pubmed:dateCreated |
1998-5-7
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|
pubmed:abstractText |
The wide range of antibody specificity and affinity results from the differing shapes and chemical compositions of their binding sites. These shapes range from discrete grooves in antibodies elicited by linear oligomers of nucleotides and carbohydrates to shallow depressions or flat surfaces for accommodation of proteins, peptides and large organic compounds.
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pubmed:grant |
|
|
pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
1380-2933
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:volume |
3
|
|
pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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|
pubmed:pagination |
253-70
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|
pubmed:dateRevised |
2007-11-14
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|
pubmed:meshHeading |
pubmed-meshheading:9530559-Amino Acid Sequence,
pubmed-meshheading:9530559-Antibody Affinity,
pubmed-meshheading:9530559-Antibody Specificity,
pubmed-meshheading:9530559-Crystallography, X-Ray,
pubmed-meshheading:9530559-Humans,
pubmed-meshheading:9530559-Immunoglobulin Fab Fragments,
pubmed-meshheading:9530559-Molecular Sequence Data,
pubmed-meshheading:9530559-Protein Conformation,
pubmed-meshheading:9530559-Structure-Activity Relationship,
pubmed-meshheading:9530559-Tetanus Toxoid
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|
pubmed:year |
1998
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|
pubmed:articleTitle |
Three-dimensional structure of a human Fab with high affinity for tetanus toxoid.
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|
pubmed:affiliation |
Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
