X-ray studies of crystalline complexes involving amino acids. II. The crystal structure of L-arginine L-glutamate

AbstractOver the past decade, the Rosetta biomolecular modeling suite has informed diverse biological questions and engineering challenges ranging from interpretation of low-resolution structural data to design of nanomaterials, protein therapeutics, and vaccines. Central to Rosetta’s success is the energy function: amodel parameterized from small molecule and X-ray crystal structure data used to approximate the energy associated with each biomolecule conformation. This paper describes the mathematical models and physical concepts that underlie the latest Rosetta energy function, beta_nov15. Applying these concepts,we explain how to use Rosetta energies to identify and analyze the features of biomolecular models.Finally, we discuss the latest advances in the energy function that extend capabilities from soluble proteins to also include membrane proteins, peptides containing non-canonical amino acids, carbohydrates, nucleic acids, and other macromolecules.

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Synthesis and Crystal Structure Determination of Cyclosporin H

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc20001317 ◽

2000 ◽

Vol 65 (8) ◽

pp. 1317-1328 ◽

Cited By ~ 7

Author(s):

Alexandr Jegorov ◽

Ladislav Cvak ◽

Aleš Husek ◽

Petr Šimek ◽

Anna Heydová ◽

...

Keyword(s):

Crystal Structure ◽

Amino Acids ◽

Monoclinic Space Group ◽

X Ray Diffraction ◽

Synthesis And Crystal Structure ◽

X Ray ◽

Acid Catalyzed ◽

Products Of Reaction ◽

Cyclosporin H

Acid-catalyzed degradation of cyclosporin A was studied in various solvents and products of reaction were monitored by HPLC. Identification of amino acids and their chirality were determined after hydrolysis and derivatization by GC-MS. Cyclosporin H was isolated as the principal product and its structure was determined by X-ray diffraction: Cyclosporin H- diethyl ether-water (1 : 0.5 : 1) crystallizes in the monoclinic space group I2 with a = 12.338(2) Å, b = 18.963(2) Å, c = 34.074(3) Å, β = 96.47(2)°, Z = 4, and V = 7 921.4(17) Å3.

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Are gamma amino acids promising tools of crystal engineering? – Multicomponent crystals of baclofen

CrystEngComm ◽

10.1039/c5ce01383f ◽

2015 ◽

Vol 17 (43) ◽

pp. 8264-8272 ◽

Cited By ~ 5

Author(s):

Nikoletta B. Báthori ◽

Ornella E. Y. Kilinkissa

Keyword(s):

Crystal Structure ◽

Thermal Analysis ◽

Amino Acids ◽

Crystal Engineering ◽

Sulfonic Acid ◽

Dicarboxylic Acids ◽

Monocarboxylic Acids ◽

X Ray ◽

Toluene Sulfonic Acid

The crystal structure, thermal analysis and powder X-ray analysis of the multicomponent crystals formed between baclofen and selected monocarboxylic acids, dicarboxylic acids and p-toluene sulfonic acid are presented.

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Crystal structure of glycosyltrehalose synthase fromSulfolobus shibataeDSM5389

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x1801453x ◽

2018 ◽

Vol 74 (11) ◽

pp. 741-746

Author(s):

Nobuo Okazaki ◽

Michael Blaber ◽

Ryota Kuroki ◽

Taro Tamada

Keyword(s):

Crystal Structure ◽

Amino Acids ◽

Catalytic Mechanism ◽

Catalytic Domain ◽

Structural Basis ◽

Hyperthermophilic Archaeon ◽

X Ray ◽

X Ray Crystallography ◽

Sulfolobus Shibatae ◽

Glucosidic Bond

Glycosyltrehalose synthase (GTSase) converts the glucosidic bond between the last two glucose residues of amylose from an α-1,4 bond to an α-1,1 bond, generating a nonreducing glycosyl trehaloside, in the first step of the biosynthesis of trehalose. To better understand the structural basis of the catalytic mechanism, the crystal structure of GTSase from the hyperthermophilic archaeonSulfolobus shibataeDSM5389 (5389-GTSase) has been determined to 2.4 Å resolution by X-ray crystallography. The structure of 5389-GTSase can be divided into five domains. The central domain contains the (β/α)8-barrel fold that is conserved as the catalytic domain in the α-amylase family. Three invariant catalytic carboxylic amino acids in the α-amylase family are also found in GTSase at positions Asp241, Glu269 and Asp460 in the catalytic domain. The shape of the catalytic cavity and the pocket size at the bottom of the cavity correspond to the intramolecular transglycosylation mechanism proposed from previous enzymatic studies.

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A one-pot three carbon decarboxylative ring expansion of cyclic secondary amino acids. X-Ray crystal structure of a substituted 1-azacyclo-octa-2,4-diene

Journal of the Chemical Society Chemical Communications ◽

10.1039/c39870001296 ◽

1987 ◽

pp. 1296 ◽

Cited By ~ 19

Author(s):

Harriet Ardill ◽

Ronald Grigg ◽

Visuvanathar Sridharan ◽

John Malone

Keyword(s):

Crystal Structure ◽

Amino Acids ◽

Ring Expansion ◽

One Pot ◽

X Ray ◽

Secondary Amino ◽

Substituted 1

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Transformation of the Carboxyl Group of an Amino Acid to Variously Substituted Imidazoles through a Davidson-Type Heterocyclization

Synthesis ◽

10.1055/s-0037-1612084 ◽

2019 ◽

Vol 51 (09) ◽

pp. 1961-1968 ◽

Cited By ~ 1

Author(s):

Jim Küppers ◽

Michaela Hympánová ◽

Tim Keuler ◽

Andreas Schneider ◽

Gregor Schnakenburg ◽

...

Keyword(s):

Crystal Structure ◽

Amino Acids ◽

Amino Acid ◽

Carboxylic Acid ◽

Building Blocks ◽

Carboxyl Group ◽

Amino Group ◽

Combinatorial Approach ◽

X Ray ◽

Imidazole Derivatives

The modification of amino acids leads to valuable building blocks for the synthesis of bioactive compounds. By keeping the amino group protected, the carboxylic acid functionality can be converted in two steps into an imidazole moiety via a Davidson-like heterocyclization. This reaction allows for a combinatorial approach, in which two positions at the heterocycle can be modified. Herein, we report the synthesis of such imidazole derivatives by employing N-protected cyclohexylalanine as the starting material. Different α-halo ketones were used and two points of diversity, positions 4 and 5, were examined. The structure of the final imidazole derivatives was confirmed by three X-ray crystal structure analyses and their protease inhibiting activities were evaluated.

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Notizen: Die Kristallstruktur des Mauritins-A / The Crystal Structure of Mauritine-A

Zeitschrift für Naturforschung B ◽

10.1515/znb-1976-0231 ◽

1976 ◽

Vol 31 (2) ◽

pp. 279-280 ◽

Cited By ~ 4

Author(s):

A. Kibfel ◽

G. Will ◽

R. Tschesche ◽

H. Wilhelm

Keyword(s):

Crystal Structure ◽

Amino Acids ◽

Ring System ◽

Membered Ring ◽

Trans Configuration ◽

X Ray Diffraction ◽

Uv Spectrum ◽

X Ray ◽

Cyclopeptide Alkaloid ◽

Hydroxy Proline

The constitution and conformation of the known cyclopeptide alkaloid mauritine-A were determined by X-ray diffraction methods. All amino acids belong to the L-series, 3-hydroxy proline has trans-configuration. As indicated by the UV-spectrum, the 14-membered ring system is considerably strained.

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