Document Detail


Circular dichroism spectra of short, fixed-nucleus alanine helices.
MedLine Citation:
PMID:  12427967     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Very short alanine peptide helices can be studied in a fixed-nucleus, helix-forming system [Siedlicka, M., Goch, G., Ejchart, A., Sticht, H. & Bierzynski, A. (1999) Proc. Natl. Acad. Sci. USA 96, 903-908]. In a 12-residue sequence taken from an EF-hand protein, the four C-terminal peptide units become helical when the peptide binds La(3+), and somewhat longer helices may be made by adding alanine residues at the C terminus. The helices studied here contain 4, 8, or 11 peptide units. Surprisingly, these short fixed-nucleus helices remain almost fully helical from 4 to 65 degrees C, according to circular dichroism results reported here, and in agreement with titration calorimetry results reported recently. These peptides are used here to define the circular dichroism properties of short helices, which are needed for accurate measurement of helix propensities. Two striking properties are: (i) the temperature coefficient of mean peptide ellipticity depends strongly on helix length; and (ii) the intensity of the signal decreases much less rapidly with helix length, for very short helices, than supposed in the past. The circular dichroism spectra of the short helices are compared with new theoretical calculations, based on the experimentally determined direction of the NV(1) transition moment.
Authors:
Der-Hang Chin; Robert W Woody; Carol A Rohl; Robert L Baldwin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2002-11-11
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  99     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2002 Nov 
Date Detail:
Created Date:  2002-11-27     Completed Date:  2003-01-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15416-21     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Beckman Center, Stanford University Medical Center, CA 94305, USA.
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MeSH Terms
Descriptor/Qualifier:
Alanine / chemistry*
Circular Dichroism*
Oligopeptides / chemistry
Peptides / chemistry*
Protein Structure, Secondary
Temperature
Grant Support
ID/Acronym/Agency:
GM22994/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Oligopeptides; 0/Peptides; 25191-17-7/polyalanine; 56-41-7/Alanine
Comments/Corrections

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