Stereoselection in designed three-helix bundle metalloproteins

The stereochemical consequences of the metal‐ion assisted self‐assembly of parallel three‐helix peptide bundles are investigated. Chiral induction in the self‐assembly of systems containing extensive protein secondary structure is compared with the racemic synthesis of short metallopeptides. Isolati...

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Published inChirality (New York, N.Y.) Vol. 10; no. 1-2; pp. 35 - 40
Main Authors Case, Martin A., Ghadiri, M. Reza, Mutz, Mitchell W., Mc Lendon, George L.
Format Journal Article
LanguageEnglish
Published New York John Wiley & Sons, Inc 1998
Subjects
Circular Dichroism
de novo design
diastereoselection
Entropy
Iron - chemistry
Magnetic Resonance Spectroscopy
metalloproteins
Metalloproteins - chemical synthesis
Metalloproteins - chemistry
Peptides - chemical synthesis
Peptides - chemistry
Protein Conformation
Ruthenium - chemistry
self-assembly
Stereoisomerism
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Summary:The stereochemical consequences of the metal‐ion assisted self‐assembly of parallel three‐helix peptide bundles are investigated. Chiral induction in the self‐assembly of systems containing extensive protein secondary structure is compared with the racemic synthesis of short metallopeptides. Isolation and characterization of the individual stereoisomers of an exchange‐inert metalloprotein provide structural insights into analogous exchange‐labile systems. Chirality 10:35–40, 1998. © 1998 Wiley‐Liss,Inc.
Bibliography:ark:/67375/WNG-PBHX5VST-H
ArticleID:CHIR7
istex:6994DF0B821B97197FEB436B7F6D6EAF98FBF32D
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0899-0042
1520-636X
DOI:10.1002/chir.7