Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Equilibrium unfolding of the poly(glutamic acid)20 helix.

Equilibrium unfolding of the poly(glutamic acid)20 helix. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Equilibrium unfolding of the poly(glutamic acid)20 helix. Abstract Text:

    john m finkeJohn M Finke,patricia a jenningsPatricia A Jennings,jennifer c leeJennifer C Lee, onuchic Onuchic,jay r winklerJay R Winkler,

    The equilibrium structural ensemble of a 20-residue polyglutamic acid peptide (E(20)) was studied with FRET, circular dichroism, and molecular dynamics (MD) simulations. A FRET donor, o-aminobenzamide, and acceptor, 3-nitrotyrosine, were introduced at the N- and C-termini, respectively. Circular dichroism, steady state FRET, and time-resolved FRET measurements were employed to characterize the fraction helix and end-to-end distance under different pH conditions: pH 4 (60% alpha-helix), pH 6 (0% alpha-helix), and pH 9 (0% alpha-helix). At pH 4, the end-to-end distance was measured at 24 A and determined to be considerably less than the 31 A predicted for an alpha-helix of the same length. At pH 6 and 9, the end-to-end distance was measured at > 31 and 39 A respectively, both which are determined to be considerably greater than the 27 A predicted for a freely jointed random coil of the same length. To better understand the physical forces underlying the unusual helix-coil transition in this peptide, three theoretical MD models of E(20) were constructed: (1) a pure alpha-helix, (2) an alpha-helix with equivalent attractive intramolecular contacts, and (3) a weak alpha-helix with termini-weighted intramolecular contacts ("sticky ends"). Using MD simulations, the bent helix structure calculated from Model 3 was found to be the closest in agreement with the experimental data.

    Equilibrium unfolding of the poly(glutamic acid)20 helix. Publishing Authors By Initials

    jm finkeJM Finke,pa jenningsPA Jennings,jc leeJC Lee,jn onuchicJN Onuchic,jr winklerJR Winkler,

    For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

    PUBMED ID PMID:

    MEDLINE DATE:

    Equilibrium unfolding of the poly(glutamic acid)20 helix. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Biopolymers

    VOLUME: 86

    Page Numbers: 193-211

    Journal Abbreviation: Biopolymers

    ISSN: 0006-3525

    DAY: 15

    MONTH: Jun

    YEAR: 2007

    Equilibrium unfolding of the poly(glutamic acid)20 helix. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 372525

    Equilibrium unfolding of the poly(glutamic acid)20 helix. Keywords Mesh Terms:

    KEYWORDS: Temperature

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Equilibrium unfolding of the poly(glutamic acid)20 helix. Information

    Substance Name: Polyglutamic Acid

    Registry Number: 25513-46-6

    Grant and Affiliation Information for Equilibrium unfolding of the poly(glutamic acid)20 helix.

    AFFILIATION: Department of Chemistry, Oakland University, Rochester, MI 48309-4477, USA. finke@oakland.edu

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM54038

    ACRONYM: GM

    MEDLINETA: Biopolymers

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Equilibrium unfolding of the polyglutamic acid20 helix Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News