Computational studies on the backbone‐dependent side‐chain orientation induced by the (S,S)‐CXC motif
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Summary
It is concluded that cyclization has a great impact on the synplanar orientation of the X and Y side chains in the (S,S)Ac‐XCYC‐NH2 series of compounds while charge–charge interaction has only a weak synergic effect.
- Type
- article
- Published
- 2008-12-01
- Cited by
- 7
- References
- 34
- Access
- Open access
- OpenAlex
- https://openalex.org/W2010323170
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:32763979
Keywords
Side chain, Chemistry, Residue (chemistry), Stereochemistry, Alanine
References
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- Highly constrained cyclic (S,S) ‐CXaaC‐ peptides as inhibitors of fibrinogen binding to platelets
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- The CXXC motif: a rheostat in the active site.
- Rotamer libraries in the 21st century.
- Recent advances in the development and application of implicit solvent models in biomolecule simulations.
- MOLMOL: a program for display and analysis of macromolecular structures.
- A three-residue cyclic scaffold of non-RGD containing peptide analogues as platelet aggregation inhibitors: design, synthesis, and structure--function relationships.
- Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: a new homology modeling tool.
- Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP.
- The relative orientation of the Arg and Asp side chains defined by a pseudodihedral angle as a key criterion for evaluating the structure–activity relationship of RGD peptides
- Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides.
- Analysis of the RGD sequence in protein structures: comparison to the conformations of the RGDW and DRGDW peptides determined by molecular dynamics simulations
- Peptides and peptidomimetics in medicine, surgery and biotechnology.
- A classification of disulfide patterns and its relationship to protein structure and function
- Design of beta-turn based therapeutic agents.
- The CXXC motif at the N terminus of an alpha-helical peptide.
- Analysis of disulphide bond connectivity patterns in protein tertiary structure.
Cited by
- Computational modelling and molecular dynamics simulations of a cyclic peptide mimotope of the CD52 antigen complexed with CAMPATH-1H antibody
- Conformational Studies of the 313-320 and 313-332 Peptide Fragments Derived from the αIIb Subunit of Integrin Receptor with Molecular Dynamics Simulations
- Molecular dynamics simulation of antimicrobial peptide arenicin‐2: β‐Hairpin stabilization by noncovalent interactions
- A highly constrained cyclic (S,S)-CDC- peptide is a potent inhibitor of carotid artery thrombosis in rabbits
- Insights into the structure of the PmrD protein with molecular dynamics simulations.
- Conformation dynamics of cyclic disulfides and selenosulfides in CXXC(U) (X = Gly, Ala) tetrapeptide redox motifs
- New peptides Lightening proteasome activators and compositions containing them
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