Literature DB >> 6892782

Proton magnetic resonance study of crambin, a hyperstable hydrophobic protein, at 250 and 600 MHz.

M Llinás, A De Marco, J T Lecomte.   

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Year:  1980        PMID： 6892782     DOI： 10.1021/bi00547a016

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  4 in total

1.  Solvent and temperature effects on crambin, a hydrophobic protein.

Authors:  M Llinás; J T Lecomte; A De Marco
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

2.  Reminiscence: Miguel Llinás (1938-2020) : The Lasting Gifts of a Tireless Mentor.

Authors:  Juliette T J Lecomte
Journal:  Protein J       Date:  2021-06-05       Impact factor: 2.371

3.  Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur.

Authors:  Wayne A Hendrickson; Martha M Teeter
Journal:  Nature       Date:  1981-03-12       Impact factor: 49.962

4.  SDS-resistant aggregation of membrane proteins: application to the purification of the vesicular monoamine transporter.

Authors:  C Sagné; M F Isambert; J P Henry; B Gasnier
Journal:  Biochem J       Date:  1996-06-15       Impact factor: 3.857
  4 in total

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