Structures of <scp>L</scp>-prolylsarcosine monohydrate and <i>tert</i>-butoxycarbonyl-<scp>L</scp>-prolylsarcosine benzyl ester

Kojima, Takuji; Kido, Takuhei; Itoh, Hiroshi; Yamane, T.; Ashida, Tamaichi

doi:10.1107/s0567740880003196

Cited by 11 publications

(1 citation statement)

References 4 publications

(4 reference statements)

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“…d Number of antiparallel/hybrid/unique structures for other types of layers. e Pro-Sar (Kojima et al, 1980). f Number of Val-Ala class (Gö rbitz, 2003a)/others for structures without layers.…”

Section: Structure From Sequencementioning

confidence: 99%

Structures of dipeptides: the head-to-tail story

Görbitz

2010

Acta Crystallogr B Struct Sci

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The hydrogen-bonding patterns in crystal structures of unprotected, zwitterionic dipeptides are dominated by head-to-tail chains involving the N-terminal amino groups and the C-terminal carboxylate groups. Patterns that include two concomitant chains, thus generating a hydrogen-bonded layer, are of special interest. A comprehensive survey shows that dipeptide structures can conveniently be divided into only four distinct patterns, differing by definition in the symmetry of the head-to-tail chains and amide hydrogen-bonding type, but also in other properties such as peptide conformation and the propensity to include solvent water or various organic guest molecules. Upon crystallization, the choice of pattern for a specific dipeptide is not random, but follows from the amino acid sequence.

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Section: Structure From Sequencementioning

confidence: 99%

Structures of dipeptides: the head-to-tail story

Görbitz

2010

Acta Crystallogr B Struct Sci

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Calibration of effective van der Waals atomic contact radii for proteins and peptides

1987

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Effective van der Waals radii were calibrated in such a way that molecular models built from standard bond lengths and bond angles reproduced the amino acid conformations observed by crystallography in proteins and peptides. The calibrations were based on the comparison of the Ramachandran plots prepared from high-resolution X-ray data of proteins and peptides with the allowed phi, psi torsional angle space for the dipeptide molecular models. The calibrated radii are useful as criteria with which to filter energetically improbable conformations in molecular modeling studies of proteins and peptides.

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Synthesis and conformation of cyclic hexapeptide cyclo(Pro-Sar-Sar)2

Kimura

Imanishi

1981

International Journal of Biological Macromolecules

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Structures of L-prolylsarcosine monohydrate and tert-butoxycarbonyl-L-prolylsarcosine benzyl ester

Cited by 11 publications

References 4 publications

Structures of dipeptides: the head-to-tail story

Structures of dipeptides: the head-to-tail story

Calibration of effective van der Waals atomic contact radii for proteins and peptides

Synthesis and conformation of cyclic hexapeptide cyclo(Pro-Sar-Sar)2

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