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- W2005471138 endingPage "419" @default.
- W2005471138 startingPage "396" @default.
- W2005471138 abstract "The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral alpha-amino acids with a quaternary alpha-carbon atom, as determined by conformational energy computations, crystal-state (x-ray diffraction) analyses, and solution ((1)H-NMR and spectroscopic) investigations, are reviewed. It is concluded that 3(10)/alpha-helical structures and the fully extended (C(5)) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C(alpha) (i) <--> C(alpha) (i) cyclized) of their side chains. The intriguing relationship between alpha-carbon chirality and bend/helix handedness is also illustrated. gamma-Bends and semiextended conformations are rarely observed. Formation of beta-sheet structures is prevented." @default.
- W2005471138 created "2016-06-24" @default.
- W2005471138 creator A5032879706 @default.
- W2005471138 creator A5040500402 @default.
- W2005471138 creator A5065741079 @default.
- W2005471138 creator A5078323087 @default.
- W2005471138 date "2001-01-01" @default.
- W2005471138 modified "2023-10-16" @default.
- W2005471138 title "Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)" @default.
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