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CamSol specifications


Unique identifier OMICS_11321
Name CamSol
Interface Web user interface
Restrictions to use Academic or non-commercial use
Computer skills Basic
Stability Stable
Maintained Yes


  • person_outline Michele Vendruscolo <>

Publication for CamSol

CamSol in publications

PMCID: 5916882
PMID: 29695721
DOI: 10.1038/s41467-018-04078-y

[…] substates are characterized by a significantly lower β-sheet content (~38 and 30% for wt and d76n, respectively).fig. 4, an analysis of the predicted solubility of the two ensembles performed with camsol shows that the d76n mutation in the sequence causes a small reduction of the solubility for residues 74–77 (supplementary fig. ). the solubility profiles corrected for the structure […]

PMCID: 5900942
PMID: 29315487
DOI: 10.1002/bit.26543

[…] ), and pasta (trovato, seno, & tosatto, ) can be used to predict the presence of aggregation‐prone regions (aprs) within proteins using protein primary sequence information alone. in addition, camsol (sormanni, aprile, & vendruscolo, ) and sap can be used to predict aggregation‐prone (poorly soluble) surface‐exposed regions (chennamsetty, voynov, kayser, helk, & trout, ; trainor, […]

PMCID: 5573320
PMID: 28842596
DOI: 10.1038/s41598-017-09749-2

[…] of mutations simultaneously, based on the results of multiple sequence alignment (msa) and structural data, . in addition, hotspots can be predicted using software such as aggrescan, solubis, and camsol., for such difficult cases, learning from successful examples in previous research would facilitate development of a new method of estimation. in a previous study, we discovered a phenomenon […]

PMCID: 5558012
PMID: 28811609
DOI: 10.1038/s41598-017-07800-w

[…] laboratory-constructed library, have a high degree of sequence similarity, methods of predicting solubility changes upon mutation are particularly well-suited for this purpose. in this context, the camsol method of predicting solubility changes upon mutations, and in particular the sequence-based intrinsic solubility score, may be particularly helpful. to test this strategy, in this work […]

PMCID: 5518135
PMID: 28724440
DOI: 10.1186/s12934-017-0738-1

[…] before transporting through sec secretion system. also, unfolded α-amylase is less soluble than folded one because we find α-amylase precursor (accession number h9bpx5) poorly soluble when using camsol [] to compute its solubility (fig. ).fig. 1 , although prsa serves as a post-translocation chaperone to help the folding of secreted proteins and similar chaperones, peptidyl-prolyl cis/trans […]

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CamSol institution(s)
Department of Chemistry, University of Cambridge, Cambridge, UK

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