Document Detail

A propensity scale for type II polyproline helices (PPII): aromatic amino acids in proline-rich sequences strongly disfavor PPII due to proline-aromatic interactions.
MedLine Citation:
PMID:  22667692     Owner:  NLM     Status:  MEDLINE    
Type II polyproline helices (PPII) are a fundamental secondary structure of proteins, common in globular and nonglobular regions and important in cellular signaling. We developed a propensity scale for PPII using a host-guest system with sequence Ac-GPPXPPGY-NH(2), where X represents any amino acid. We found that proline has the highest PPII propensity, but most other amino acids display significant PPII propensities. The PPII propensity of leucine was the highest of all propensities of non-proline residues. Alanine and residues with linear side chains displayed the next highest PPII propensities. Three classes of residues displayed lower PPII propensities: β-branched amino acids (Thr, Val, and Ile), short amino acids with polar side chains (Asn, protonated Asp, Ser, Thr, and Cys), and aromatic amino acids (Phe, Tyr, and Trp). tert-Leucine particularly disfavored PPII. The basis of the low PPII propensities of aromatic amino acids in this context was significant cis-trans isomerism, with proline-rich peptides containing aromatic residues exhibiting 45-60% cis amide bonds, due to Pro-cis-Pro-aromatic and aromatic-cis-Pro amide bonds.
Alaina M Brown; Neal J Zondlo
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-06-14
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-06-26     Completed Date:  2012-09-06     Revised Date:  2014-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5041-51     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Amino Acids, Aromatic / chemistry*,  metabolism
Caenorhabditis elegans
Molecular Sequence Data
Peptides / chemistry*
Proline / chemistry*,  metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Grant Support
Reg. No./Substance:
0/Amino Acids, Aromatic; 0/Peptides; 25191-13-3/polyproline; 9DLQ4CIU6V/Proline

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