Review Reports

Round 1

Reviewer 1 Report

In this work, the authors studied RNase A oligomerization and in detail structural and/or functional properties associtaed to two different protocols tested. Data and strategies are well presented and discussed.

Some minor comments for the paper are mentioned below:

• Stability of RNase A species should also be evaluated in the presence of chemical denaturants;
• Toxicity on tumoral cells would require at least one other cell line;
• Discussion paragraph is too long and speculative;

 

Moreover, there are some typographical errors, or venial inaccuracies, to correct:

Ex:

• In paragraph 2.11, page 5, please add "o" to "tw";
• In the legend of figure 5, lyophlization must be replaced with lyophilization;
• Verbs in the present and past tense are often used in the same paragraphs (see paragraphs 2.6, 3.5
• in the legends of figures 3 and 4, pH values of the buffers should be added
• In the title of paragraph 3.9, "on human melanoma" is more appropriate than "in human melanoma" 

 

 

Author Response

Please see the attachment

Author Response File: Author Response.pdf

Reviewer 2 Report

The ability of RNase A to oligomerize through domain swapping has been one of the most intriguing phenomena discovered in the early years of structural biology.  Since then, this aspect has been the subject  by a remarkable number of studies. In this scenario, Gotte and coworkers report a comparative analysis of the biophysical and functional properties of domain-swapped RNase A dimers obtained using different experimental protocols. Considering that the topic is of interest, that the experiments are technically sound and that the manuscript is clearly written, I personally believe that this work can be considered for publication. I would suggest a mention either in the Introduction or in the Discussion to the RNaseA mutants that favor oligomerization.

Minor point

In line 243 “tw “  should be “two”

Author Response

Please see the attachment

Author Response File: Author Response.pdf