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Literature DB >> 12418101

Unfolded proteins studied by Raman optical activity.

L D Barron¹, E W Blanch, L Hecht.

Abstract

Mesh：

Substances：
Proteins

Year: 2002 PMID： 12418101 DOI： 10.1016/s0065-3233(02)62005-4

Source DB: PubMed Journal: Adv Protein Chem ISSN： 0065-3233

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Cited

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9 in total

1. Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease.

Authors: Roger S Armen; Mari L DeMarco; Darwin O V Alonso; Valerie Daggett
Journal: Proc Natl Acad Sci U S A Date: 2004-07-27 Impact factor: 11.205

2. Further evidence for the absence of polyproline II stretch in the XAO peptide.

Authors: Joanna Makowska; Sylwia Rodziewicz-Motowidlo; Katarzyna Baginska; Mariusz Makowski; Jorge A Vila; Adam Liwo; Lech Chmurzynski; Harold A Scheraga
Journal: Biophys J Date: 2007-02-02 Impact factor: 4.033

3. Optical signatures of molecular dissymmetry: combining theory with experiments to address stereochemical puzzles.

Authors: Parag Mukhopadhyay; Peter Wipf; David N Beratan
Journal: Acc Chem Res Date: 2009-06-16 Impact factor: 22.384

4. Characterizing aqueous solution conformations of a peptide backbone using Raman optical activity computations.

Authors: Parag Mukhopadhyay; Gérard Zuber; David N Beratan
Journal: Biophys J Date: 2008-09-19 Impact factor: 4.033

5. Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix.

Authors: Catherine M Templeton; Saeideh Ostovar pour; Jeanette R Hobbs; Ewan W Blanch; Steven D Munger; Graeme L Conn
Journal: Chem Senses Date: 2011-02-22 Impact factor: 3.160

Unfolded proteins studied by Raman optical activity.

1. Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease.

2. Further evidence for the absence of polyproline II stretch in the XAO peptide.

3. Optical signatures of molecular dissymmetry: combining theory with experiments to address stereochemical puzzles.

4. Characterizing aqueous solution conformations of a peptide backbone using Raman optical activity computations.

5. Reduced sweetness of a monellin (MNEI) mutant results from increased protein flexibility and disruption of a distant poly-(L-proline) II helix.

6. A statistical analysis of the PPII propensity of amino acid guests in proline-rich peptides.

7. Determination of protein fold class from Raman or Raman optical activity spectra using random forests.

Review 8. Local order in the unfolded state: conformational biases and nearest neighbor interactions.

9. Secondary Structure and Glycosylation of Mucus Glycoproteins by Raman Spectroscopies.