Discovering protein secondary structures: Classification and description of isolated α‐turns
Identifieur interne : 002917 ( Main/Merge ); précédent : 002916; suivant : 002918Discovering protein secondary structures: Classification and description of isolated α‐turns
Auteurs : Vincenzo Pavone [Italie] ; Girolamo Gaeta [Italie] ; Angela Lombardi [Italie] ; Flavia Nastri [Italie] ; Ornella Maglio [Italie] ; Carla Isernia [Italie] ; Michele Saviano [Italie]Source :
- Biopolymers [ 0006-3525 ] ; 1996-06.
English descriptors
- KwdEn :
- 5acn, Amino, Amino acid, Amino acid frequency, Amino acid residue, Amino acid residues, Aturns, Average structures, Average values, Backbone, Backbone atom superimposition, Backbone atoms, Basic motifs, Biol, Central positions, Central residues, Chain reversal, Chem, Conformation, Consecutive angles, Corresponding backbone mirror images, Data base, Different peptide bond orientation, Different types, Dipole interaction, Electrostatic contributions, Electrostatic interaction, First residue, Further calculations, Glutamic acid, Helix, High frequency, Hydrogen bond, Identical sequences, Intercluster rmsd, Intercluster rmsds, Lgdl, Loop side, Lova, Lprc, Mirror image, Mirror images, Ofthe, Other dipoles, Other type, Overwhelming presence, Pentapeptide sequences, Peptide, Peptide bond, Peptide bonds, Peptide plane, Previous page, Proline residues, Protein, Protein chem, Protein data bank, Protein structure, Protein structures, Protein surface, Ramachandran plots, Relative orientation, Residue, Reversal, Secondary structures, Sequence protein, Standard deviations, Stereo view, Third residue, Torsion angles, Total number, Trans peptide bonds.
- Teeft :
- 5acn, Amino, Amino acid, Amino acid frequency, Amino acid residue, Amino acid residues, Aturns, Average structures, Average values, Backbone, Backbone atom superimposition, Backbone atoms, Basic motifs, Biol, Central positions, Central residues, Chain reversal, Chem, Conformation, Consecutive angles, Corresponding backbone mirror images, Data base, Different peptide bond orientation, Different types, Dipole interaction, Electrostatic contributions, Electrostatic interaction, First residue, Further calculations, Glutamic acid, Helix, High frequency, Hydrogen bond, Identical sequences, Intercluster rmsd, Intercluster rmsds, Lgdl, Loop side, Lova, Lprc, Mirror image, Mirror images, Ofthe, Other dipoles, Other type, Overwhelming presence, Pentapeptide sequences, Peptide, Peptide bond, Peptide bonds, Peptide plane, Previous page, Proline residues, Protein, Protein chem, Protein data bank, Protein structure, Protein structures, Protein surface, Ramachandran plots, Relative orientation, Residue, Reversal, Secondary structures, Sequence protein, Standard deviations, Stereo view, Third residue, Torsion angles, Total number, Trans peptide bonds.
Abstract
Irregular protein secondary structures are believed to be important structural domains involved in molecular recognition processes between proteins, in interactions between peptide substrates and receptors, and in protein folding. In these respects tight turns are being studied in detail. They also represent template structures for the design of new molecules such as drugs, pesticides, or antigens. Isolated α‐turns, not participating in α‐helical structures, have received little attention due to the overwhelming presence of other types of tight turns in peptide and protein structures. The growing number of protein X‐ray structures allowed us to undertake a systematic search into the Protein Data Bank of this uncharacterized protein secondary structure. A classification of isolated α‐turns into different types, based on conformational similarity, is reported here. A preliminary analysis on the occurrence of some particular amino acids in certain positions of the turned structure is also presented. © 1996 John Wiley & Sons, Inc.
Url:
DOI: 10.1002/(SICI)1097-0282(199606)38:6<705::AID-BIP3>3.0.CO;2-V
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ISTEX:1D7F85A57382D755D7BD3A232642459168725503Le document en format XML
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<front><div type="abstract" xml:lang="en">Irregular protein secondary structures are believed to be important structural domains involved in molecular recognition processes between proteins, in interactions between peptide substrates and receptors, and in protein folding. In these respects tight turns are being studied in detail. They also represent template structures for the design of new molecules such as drugs, pesticides, or antigens. Isolated α‐turns, not participating in α‐helical structures, have received little attention due to the overwhelming presence of other types of tight turns in peptide and protein structures. The growing number of protein X‐ray structures allowed us to undertake a systematic search into the Protein Data Bank of this uncharacterized protein secondary structure. A classification of isolated α‐turns into different types, based on conformational similarity, is reported here. A preliminary analysis on the occurrence of some particular amino acids in certain positions of the turned structure is also presented. © 1996 John Wiley & Sons, Inc.</div>
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