Document Detail

A Propensity Scale for Type II Polyproline Helices: Aromatic Amino Acids in Proline-Rich Sequences Strongly Disfavor PPII Due to Proline-Aromatic Interactions.
MedLine Citation:
PMID:  22667692     Owner:  NLM     Status:  Publisher    
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 of sequence Ac-GPPXPPGY-NH2, 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 among all non-proline residues. Alanine and residues with linear side chains displayed the next highest PPII propensities. Three classes of residues displayed lower PPII propensities: beta-branched amino acids (Thr, Val, Ile); short amino acids with polar side chains (Asn, protonated Asp, Ser, Thr, Cys), and aromatic amino acids (Phe, Trp, Tyr). Tert-leucine particularly disfavored PPII. The basis of the low PPII propensities of aromatic amino acids was significant cis-trans isomerism, with proline-rich peptides containing aromatic residues exhibiting 45%-60% cis amide bond, due to Pro-cis-Pro-aromatic and aromatic-cis-Pro amide bonds.
Alaina M Brown; Neal J Zondlo
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-6-5
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  -     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-6-6     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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