Document Detail


A model peptide with enhanced helicity.
MedLine Citation:
PMID:  2021618     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The sequence of a model monomeric peptide, acetylA(EAAAK)3Aamide was altered to expedite measurement of peptide concentration and to enhance its fractional helical content. Replacement of the N-terminal alanine residue with a tryptophan residue provides a convenient chromophore for measurement of peptide concentration without diminishing the helical content. Replacement of the three lysine residues with arginine residues enhances the helical content without loss of their electrostatic contributions. Increasing the number of EAAAR sequence units in the peptide acetylW(EAAAR)nAamide from three to five indicates that the spectral features anticipated for a completely helical peptide are closely approached.
Authors:
G Merutka; W Shalongo; E Stellwagen
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  30     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1991 Apr 
Date Detail:
Created Date:  1991-05-31     Completed Date:  1991-05-31     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4245-8     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Iowa, Iowa City 52242.
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MeSH Terms
Descriptor/Qualifier:
Alanine
Amino Acid Sequence
Circular Dichroism
Hydrogen-Ion Concentration
Molecular Sequence Data
Peptides / chemistry*
Protein Conformation
Tryptophan
Grant Support
ID/Acronym/Agency:
HE 14388//PHS HHS
Chemical
Reg. No./Substance:
0/Peptides; 56-41-7/Alanine; 73-22-3/Tryptophan

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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