Atomic Force Microscopy Investigation of Ribonuclease A

Title: Atomic Force Microscopy Investigation of Ribonuclease A

Volume: 8 Issue: 5

Author(s): Luciano Paulino da Silva

Affiliation:

Keywords: ATOMIC FORCE MICROSCOPY, RIBONUCLEASE A, Rnase

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.

Cite this article as:

da Silva Paulino Luciano, Atomic Force Microscopy Investigation of Ribonuclease A, Protein & Peptide Letters 2001; 8 (5) . https://dx.doi.org/10.2174/0929866013409292