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2000
Volume 8, Issue 5
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

Ribonuclease A (RNase A) molecules have been adsorbed onto mica surfaces from aqueous solution at pH 7.4. Atomic force microscopy (AFM) images of native RNase A show aggregates of monomers each having a diameter of 9 nm. This is consistent with a globular unit the size of which would be substantially larger than that expected for a 13-kDa protein. These experiment suggest that the RNase A oligomer subunits exist as a multimeric complex with the 13-kDa protein.

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/content/journals/ppl/10.2174/0929866013409292
2001-10-01
2025-09-01
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/content/journals/ppl/10.2174/0929866013409292
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  • Article Type:
    Review Article
Keyword(s): ATOMIC FORCE MICROSCOPY; RIBONUCLEASE A; Rnase
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