Turn structures in CGRP C-terminal analogues promote stable arrangements of key residue side chains.

Carpenter, K A; Schmidt, R; von Mentzer, B; Haglund, U; Roberts, E; Walpole, C

Carpenter, K A; Schmidt, R; von Mentzer, B; Haglund, U; Roberts, E; Walpole, C.

Affiliation

Carpenter KA; Department of Chemistry, AstraZeneca R&D Montreal, 7171 Frédérick-Banting, Saint-Laurent, Québec, Canada H4S 1Z9. katharine.carpenter@astrazeneca.com

Biochemistry ; 40(28): 8317-25, 2001 Jul 27.

Article in En | MEDLINE | ID: mdl-11444978

Subject(s)

Amino Acids/chemistry; Amino Acids/metabolism; Calcitonin Gene-Related Peptide/chemistry; Calcitonin Gene-Related Peptide/metabolism; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Alanine/metabolism; Amides; Amino Acid Sequence; Amino Acid Substitution; Humans; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular/methods; Peptide Fragments/chemical synthesis; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protons; Receptors, Calcitonin Gene-Related Peptide/metabolism; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Temperature; Tumor Cells, Cultured

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Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Calcitonin Gene-Related Peptide / Amino Acids Limits: Humans Language: En Journal: Biochemistry Year: 2001 Document type: Article Country of publication: United States

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