Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

The preference of tryptophan for membrane interfaces.

The preference of tryptophan for membrane interfaces. 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
  • The preference of tryptophan for membrane interfaces. Abstract Text:

    w m yauW M Yau,w c wimleyW C Wimley,k gawrischK Gawrisch,s h whiteS H White,

    One of the ubiquitous features of membrane proteins is the preference of tryptophan and tyrosine residues for membrane surfaces that presumably arises from enhanced stability due to distinct interfacial interactions. The physical basis for this preference is widely believed to arise from amphipathic interactions related to imino group hydrogen bonding and/or dipole interactions. We have examined these and other possibilities for tryptophan's interfacial preference by using 1H magic angle spinning (MAS) chemical shift measurements, two-dimensional (2D) nuclear Overhauser effect spectroscopy (2D-NOESY) 1H MAS NMR, and solid state 2H NMR to study the interactions of four tryptophan analogues with phosphatidylcholine membranes. We find that the analogues reside in the vicinity of the glycerol group where they all cause similar modest changes in acyl chain organization and that hydrocarbon penetration was not increased by reduction of hydrogen bonding or electric dipole interaction ability. These observations rule out simple amphipathic or dipolar interactions as the physical basis for the interfacial preference. More likely, the preference is dominated by tryptophan's flat rigid shape that limits access to the hydrocarbon core and its pi electronic structure and associated quadrupolar moment (aromaticity) that favor residing in the electrostatically complex interface environment.

    The preference of tryptophan for membrane interfaces. Publishing Authors By Initials

    wm yauWM Yau,wc wimleyWC Wimley,k gawrischK Gawrisch,sh whiteSH White,

    For similar water research abstracts see: water research

    PUBMED ID PMID:

    MEDLINE DATE:

    The preference of tryptophan for membrane interfaces. Journal Published:

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

    Journal: Biochemistry

    VOLUME: 37

    Page Numbers: 14713-8

    Journal Abbreviation: Biochemistry

    ISSN: 0006-2960

    DAY: 20

    MONTH: Oct

    YEAR: 1998

    The preference of tryptophan for membrane interfaces. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370623

    The preference of tryptophan for membrane interfaces. Keywords Mesh Terms:

    KEYWORDS: Water

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: The preference of tryptophan for membrane interfaces. Information

    Substance Name: Water

    Registry Number: 7732-18-5

    Grant and Affiliation Information for The preference of tryptophan for membrane interfaces.

    AFFILIATION: National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Rockville, Maryland 20852, USA.

    Country: UNITED STATES

    UNITED STATES Research PublicationUNITED STATES Research Publication

    AGENCY: United States NIGMS

    GRANT: GM46823

    ACRONYM: GM

    MEDLINETA: Biochemistry

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    The preference of tryptophan for membrane interfaces 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