Atomic Force Microscopy Investigation of Ribonuclease A

Author: Silva LP

Source: Protein and Peptide Letters, Volume 8, Number 5, October 2001 , pp. 343-347(5)

Publisher: Bentham Science Publishers

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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.

Keywords: ATOMIC FORCE MICROSCOPY; RIBONUCLEASE A; Rnase

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409292

Affiliations: 1: Departamento de Genetica e Morfologia, UnB, Brasilia, DF, Brazil.

Publication date: 2001-10-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.