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Preferred conformation of the terminally blocked (Aib)10homo‐oligopeptide: A long, regular 310‐helix |
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Biopolymers,
Volume 31,
Issue 1,
1991,
Page 129-138
Claudio Toniolo,
Marco Crisma,
Gian Maria Bonora,
Ettore Benedetti,
Benedetto Dl Blasio,
Vincenzo Pavone,
Carlo Pedone,
Antonello Santini,
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摘要:
AbstractThe decapeptidepBrBz‐ (Aib)10‐OtBu, synthesized by the 5(4H)‐oxazolone method, crystallizes in the monoclinic space group C2/c witha= 43.901(2),b= 9.289(2), andc= 34.746(3) A; β = 114.69(3)°; andZ= 8. The crystals contain one molecule of water associated with each peptide. The structure has been solved by the Patterson method and refined to anRvalue of 0.073 for 6819 observed reflections. The peptide adopts a regular 310‐helical structure stabilized by eight NH …︁ OC intramolecular 1 ← 4 (or C10) H bonds. This study has allowed us to characterize this important peptide secondary structure in great detail. The crystal‐state conformation agrees well with proposals made on the basis of an ir absorption and1H
ISSN:0006-3525
DOI:10.1002/bip.360310112
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1991
数据来源: WILEY
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| 12. |
Masthead |
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Biopolymers,
Volume 31,
Issue 1,
1991,
Page -
Preview
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PDF (98KB)
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ISSN:0006-3525
DOI:10.1002/bip.360310101
出版商:Wiley Subscription Services, Inc., A Wiley Company
年代:1991
数据来源: WILEY
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