Structure and conformation of L-tyrosyl-L-tyrosine dihydrate, C18H20N2O5.2H2O

Cotrait, M.; Bideau, J. P.; Beurskens, Gezina; Bosman, W. P.; Beurskens, Paul T.

doi:10.1107/s0108270184008155

Cited by 5 publications

(4 citation statements)

References 5 publications

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“…The conformation angles 1 21 and 1 22 are 133.1 (3) and À53.4 (3) and À110.1 (3) and 67.1 (4) for residues 1 and 2, respectively. These 1 21 values lie within the expected range of 90AE30 (Cotrait et al, 1984). In the case of tyrosinium residue 1, the 1 21 value deviates slightly from the expected value.…”

Section: Commentsupporting

confidence: 67%

Bis(L-tyrosinium) sulfate monohydrate

2002

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Section: Commentsupporting

confidence: 67%

Bis(L-tyrosinium) sulfate monohydrate

2002

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“…(i) Nine highly hydrated structures of dipeptides with two bulky side chains. All except Tyr-Tyr dihydrate (Cotrait et al, 1984) are clearly divided into layers, derived from S5 or more commonly from T5, as shown for Tyr-Trp hydrate in Fig. 9(d) (Gö rbitz & Hartviksen, 2008).…”

Section: Figure 10mentioning

confidence: 83%

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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“…The interactions between the terminal ÐNH 3 + and ÐCOO À groups that usually dominate the hydrogen-bonding patterns of dipeptides are missing in (1); all amino H atoms are instead accepted by solvent water molecules. Other dipeptide structures without head-to-tail chains also have cocrystallized water molecules in addition to either a charged multiple donor in the side chain [l-Arg-l-GluÁ2H 2 O (Pandit et al, 1983) and l-Arg-l-AspÁ2H 2 O (Ramakrishnan & Viswamitra, 1988) (Ramakrishnan et al, 1984), l-Tyr-l-TyrÁ2H 2 O (Cotrait et al, 1984)]. The structure of l-Tyr-l-Lys (Urpi et al, 1988) has no solvent water, but it is not directly comparable to the others as the positive charge is located in the side chain, while the main chain amino group is neutral.…”

Section: Crystal Packing Arrangement and Hydrogen Bondingmentioning

confidence: 99%

β Turns, water cage formation and hydrogen bonding in the structures of L-valyl-L-phenylalanine

Görbitz

2002

Acta Crystallogr B Struct Sci

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L-Valyl-L-phenylalanine has been crystallized as an orthorhombic dihydrate (1) in the shape of needles and as a monoclinic trihydrate (2) with Z = 16 (P2(1), Z' = 8) in the shape of thin plates. Peptide molecules in these two structures occur in three basic conformations, termed c(1), c(2A) and c(2B). c(2B) has not been observed previously for dipeptides. Together with c(1) it forms a model pair for Type I and Type II beta-turns in protein structures. The crystal packing of (2) is remarkable in that some of the L-Val side chains are exposed to the solvent region of the crystal rather than being located in a hydrophobic layer. The crystal packing thus offers a unique and detailed view of hydrogen-bond cage formation around the hydrophobic groups by the 24 cocrystallized water molecules. The eight [bond]NH(3)(+)...(-)OOC[bond] contacts in the structure are unusually short and the minimum N...O distance of 2.649 (5) A represents a new extreme limit for this type of hydrogen bond in peptide structures.

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Structure and conformation of L-tyrosyl-L-tyrosine dihydrate, C18H20N2O5.2H2O

Cited by 5 publications

References 5 publications

Bis(L-tyrosinium) sulfate monohydrate

Bis(L-tyrosinium) sulfate monohydrate

Structures of dipeptides: the head-to-tail story

β Turns, water cage formation and hydrogen bonding in the structures of L-valyl-L-phenylalanine

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