Redetermination of the crystal structure of N-acetyl glycine (2-acetamidoacetic acid), C4H7NO3

Saronjini, B. K.; Narayana, B.; Yathirajan, H. S.; Gerber, Thomas; Hosten, Eric C.

doi:10.1524/ncrs.2013.0125

Cited by 3 publications

(3 citation statements)

References 12 publications

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“…In Tables , we listed all published α‐amino acid derivatives and (either linear or, more rarely, cyclic) peptides to the decamer level where single or consecutive fully‐extended (C 5 ) structures were identified by X‐ray diffraction in the last 5/6 years. A few, still unpublished 3D‐structures, characterized by the C 5 form and solved in the Padova laboratory, are presented in Table…”

Section: Detailed Literature Survey On Peptides Since 2012mentioning

confidence: 99%

The fully‐extended conformation in peptides and proteins

et al. 2018

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The intramolecularly H‐bonded, fully‐extended conformation (C5) of an α‐amino acid residue (and the resulting 2.05‐helix obtained via its propagation) is one of the least extensively investigated types of peptide and protein backbone secondary structure. This situation does still currently occur despite its unique ability to enjoy by far the largest separation per residue among peptide conformations. In this article, we offer a detailed update of our present knowledge on this intriguing 3D‐structure of peptides in the crystal state as obtained from recently published investigations, complemented by a statistical analysis for its occurrence in the crystal structures of α‐amino acid derivatives and peptides available in the Cambridge Structural Database. We have expanded this useful information to the results of a bioinformatics analysis performed on this (so far largely unappreciated) conformation authenticated in all proteins solved by X‐ray diffraction to a resolution of ≤ 1.5 Å. In the last section, we describe the results of our DFT calculations on the conformational preferences of a set of homopeptides (from monomer to octamer) based on as many as six proteins and two noncoded, carefully selected, α‐amino acids. From this literature survey integrated by new energy calculations, we have definitely provided strong support to the thesis that this polypeptide 3D‐structure does indeed exist, it should be not neglected in future studies by structural biochemists, and it represents a very attractive, novel backbone for applications for organic, medicinal, and biomaterials chemists.

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Section: Detailed Literature Survey On Peptides Since 2012mentioning

confidence: 99%

The fully‐extended conformation in peptides and proteins

et al. 2018

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“…In continuation of our interest in the structures of carboxylic acids and their derivatives the title compound was synthesized and its structure determined. The structures of other amides determined by us are apparent in the literature [7][8][9][10][11]. The title structure shows the expected bonding pattern of an ortho-trifluoromethylanilide of hexanoic acid.…”

Section: Commentmentioning

confidence: 64%

Crystal structure of N-(2-(trifluoromethyl)phenyl)hexanamide, C₁₃H₁₆F₃NO

Hosten

Betz

2020

Zeitschrift Für Kristallographie - New Crystal Structures

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“…In continuation of our interest in the structural aspects of amides [7][8][9][10][11] we initiated a larger study aimed at elucidating the influence of sterical overcrowding on the conformation as well as bond lengths of differently substituted amides featuring aniline-derivatives as bonding partners. The title compound appeared as an interesting target molecule in this context and, therefore, we sought to determine its molecular and crystal structure.…”

Section: Commentmentioning

confidence: 99%