CCL: Capping termini - protein modeling



Maura,

capping is important if the residues, which are close to the place of truncation (consequently to the capping), have a non-negligible effect on the property you are interested in. Non-appropriate capping groups can generate artificial interactions which would not be present in the native, non-truncated protein and cover-up what really happens in the native peptide region.

You might want to read the following paper about different capping options.

http://dx.doi.org/10.1002/qua.21553

Abstract:
The accuracy of the determination of the energy of interaction between Phe20 and the Pro5-Thr6-Tyr7-Pro8 complex inside the hydrophobic core of avian pancreatic polypeptide was investigated using three capping strategies for molecular fractionation with conjugated caps and DFT quantum chemical calculations at the BHandHLYP/cc-pVTZ level of theory. The most accurate determination resulted from acetylation of the a-amino group combined with methyl amidation of the a-carbonyl group, with relative deviations less than 10%. Combinations of hydrogenation of the a-amino group with the replacement of the a-carbonyl group with a hydrogen and the hydrogenation of the a-amino group with methylation of the a-carbonyl group were less accurate, leading to relative deviations up to 35%. Choice of capping methods depends on the structural features of the polypeptide system, the desired accuracy, and the available computational resources.

Best,
Jozsef

On 09/16/2010 09:16 AM, Maura Mooney mmooney05,+,qub.ac.uk wrote:
Sent to CCL by: "Maura  Mooney" [mmooney05%a%qub.ac.uk]
 Hi,
 My question regards peptide caps. I have a few proteins (~25kDa) in which the
 first and last few residues are truncated. In what circumstances should I cap
 the protein termini, and apart from stability in small alpha helices, why should
 we cap protein termini?
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