Pinpointing disulfide connectivities in cysteine-rich proteins.

Bernardino, K; Pinto, M E F; Bolzani, V S; de Moura, A F; Batista Junior, J M

Bernardino, K; Pinto, M E F; Bolzani, V S; de Moura, A F; Batista Junior, J M.

Affiliation

Bernardino K; Department of Chemistry, Federal University of São Carlos - UFSCar, São Carlos, SP 13565-905, Brazil. joaombj@hotmail.com.

Chem Commun (Camb) ; 53(53): 7337-7340, 2017 Jun 29.

Article in En | MEDLINE | ID: mdl-28508909

ABSTRACT

ABSTRACT

A simple MD-based protocol is presented to accurately predict both the sequence and order of disulfide bond formation in proteins containing multiple cysteine residues. It provides a detailed description of their dynamical and structural features, which can be used to perform ensemble-averaged ECD calculations. Plant cyclotides are used as model compounds.

Subject(s)

Cyclotides/chemistry; Cysteine/chemistry; Disulfides/chemistry; Circular Dichroism; Molecular Dynamics Simulation; Thermodynamics; Violaceae/chemistry

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cysteine / Cyclotides / Disulfides Type of study: Prognostic_studies Language: En Journal: Chem Commun (Camb) Journal subject: QUIMICA Year: 2017 Document type: Article Affiliation country: Brazil Publication country: ENGLAND / ESCOCIA / GB / GREAT BRITAIN / INGLATERRA / REINO UNIDO / SCOTLAND / UK / UNITED KINGDOM

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