Literature DB >> 310598

Structure analysis of small proteins by electron microscopy: valinomycin, bacitracin and low molecular weight cell growth stimulators.

F P Ottensmeyer, D P Bazett-Jones, J Hewitt, G B Price.   

Abstract

Dark field electron microscopy was combined with optical filtering to study at high resolution the structure of the cyclopeptide antibiotics, bacitracin and valinomycin, and two proteins of unknown structure, LMW-CSA N and B, low molecular weight granulocyte colony stimulating activity isolated from medium conditioned with normal or leukemic leukocytes. For bacitracin and valinomycin the images faithfully represented the known structural features at a resolution of 0.5 nm or better, depicting a two-ring structure for bacitracin, as well as the position of the potassium ion in valinomycin. Both proteins of unknown structrue had at least one cyclic peptide portion. LMW-CSA N had a size of 2.0 nm, LMW-CSA B of 2.4 nm. A potential site of the calcium ionophoric activity in the latter protein was found to be in the larger of the two ring portions constituting the molecule.

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Year:  1978        PMID: 310598     DOI: 10.1016/s0304-3991(78)80040-0

Source DB:  PubMed          Journal:  Ultramicroscopy        ISSN: 0304-3991            Impact factor:   2.689


  3 in total

1.  Structure of the signal recognition particle by electron microscopy.

Authors:  D W Andrews; P Walter; F P Ottensmeyer
Journal:  Proc Natl Acad Sci U S A       Date:  1985-02       Impact factor: 11.205

2.  Enzymatic hydrolysis of cellulose: Visual characterization of the process.

Authors:  A R White; R M Brown
Journal:  Proc Natl Acad Sci U S A       Date:  1981-02       Impact factor: 11.205

3.  Structural analysis of acute-phase alpha 2-macroglobulin.

Authors:  G J Beitel; A J Luft; D E Panrucker; F L Lorscheider
Journal:  Biochem J       Date:  1986-09-01       Impact factor: 3.857

  3 in total

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