scholarly journals Macrocyclic Tetramers—Structural Investigation of Peptide-Peptoid Hybrids

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4548
Author(s):  
Claudine Nicole Herlan ◽  
Anna Sonnefeld ◽  
Thomas Gloge ◽  
Julian Brückel ◽  
Luisa Chiara Schlee ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nmr Spectroscopy ◽  
Rational Design ◽  
Structural Investigation ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Proteolytic Degradation ◽  
X Ray ◽  
X Ray Scattering

Outstanding affinity and specificity are the main characteristics of peptides, rendering them interesting compounds for basic and medicinal research. However, their biological applicability is limited due to fast proteolytic degradation. The use of mimetic peptoids overcomes this disadvantage, though they lack stereochemical information at the α-carbon. Hybrids composed of amino acids and peptoid monomers combine the unique properties of both parent classes. Rigidification of the backbone increases the affinity towards various targets. However, only little is known about the spatial structure of such constrained hybrids. The determination of the three-dimensional structure is a key step for the identification of new targets as well as the rational design of bioactive compounds. Herein, we report the synthesis and the structural elucidation of novel tetrameric macrocycles. Measurements were taken in solid and solution states with the help of X-ray scattering and NMR spectroscopy. The investigations made will help to find diverse applications for this new, promising compound class.

scholarly journals Macrocyclic Tetramers – Structural Investigation of Peptide-Peptoid Hybrids

2021 ◽  
Author(s):  
Claudine Herlan ◽  
Anna Sonnefeld ◽  
Thomas Gloge ◽  
Julian Brückel ◽  
Luisa Schlee ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Bioactive Compounds ◽  
Rational Design ◽  
Structural Investigation ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
X Ray Scattering

The determination of the three-dimensional structure is a key step for the identification of new targets as well as the rational design of bioactive compounds. Herein, we report the synthesis and the structural elucidation of novel tetrameric macrocycles. Measurements were taken in solid and solution states with the help of X-ray scattering and NMR spectroscopy. The investigations made will help to find diverse applications for this new, promising compound class.

scholarly journals Determination of the Three-dimensional Structure of Dislocations by Synchrotron White X-ray Topography Combined with a Topo-tomographic Technique

Materia Japan ◽  
2007 ◽  
Vol 46 (12) ◽  
pp. 823-823
Author(s):  
Seiji Kawado ◽  
Toshinori Taishi ◽  
Satoshi Iida ◽  
Yoshifumi Suzuki ◽  
Yoshinori Chikaura ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Tomographic Technique

Three-dimensional structure of the calcite–water interface by surface X-ray scattering

2004 ◽  
Vol 573 (2) ◽  
pp. 191-203 ◽  
Author(s):  
P. Geissbühler ◽  
P. Fenter ◽  
E. DiMasi ◽  
G. Srajer ◽  
L.B. Sorensen ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Water Interface ◽  
X Ray ◽  
Three Dimensional Structure ◽  
X Ray Scattering ◽  
Ray Scattering

Structure determination of a partially ordered layered silicate material with an NMR crystallography approach

2017 ◽  
Vol 73 (3) ◽  
pp. 184-190 ◽  
Author(s):  
Darren Henry Brouwer ◽  
Sylvian Cadars ◽  
Kathryn Hotke ◽  
Jared Van Huizen ◽  
Nicholas Van Huizen
Keyword(s):  
Nmr Spectroscopy ◽  
Structure Determination ◽  
Three Dimensional ◽  
Layered Silicate ◽  
Silicate Layer ◽  
Silicate Material ◽  
X Ray Diffraction ◽  
X Ray ◽  
Nmr Crystallography

Structure determination of layered materials can present challenges for conventional diffraction methods due to the fact that such materials often lack full three-dimensional periodicity since adjacent layers may not stack in an orderly and regular fashion. In such cases, NMR crystallography strategies involving a combination of solid-state NMR spectroscopy, powder X-ray diffraction, and computational chemistry methods can often reveal structural details that cannot be acquired from diffraction alone. We present here the structure determination of a surfactant-templated layered silicate material that lacks full three-dimensional crystallinity using such an NMR crystallography approach. Through a combination of powder X-ray diffraction and advanced 29Si solid-state NMR spectroscopy, it is revealed that the structure of the silicate layer of this layered silicate material templated with cetyltrimethylammonium surfactant cations is isostructural with the silicate layer of a previously reported material referred to as ilerite, octosilicate, or RUB-18. High-field 1H NMR spectroscopy reveals differences between the materials in terms of the ordering of silanol groups on the surfaces of the layers, as well as the contents of the inter-layer space.

scholarly journals Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics

2018 ◽  
Vol 19 (11) ◽  
pp. 3401 ◽  
Author(s):  
Ashutosh Srivastava ◽  
Tetsuro Nagai ◽  
Arpita Srivastava ◽  
Osamu Miyashita ◽  
Florence Tama
Keyword(s):  
Protein Dynamics ◽  
Computational Methods ◽  
Protein Structures ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray ◽  
X Ray Crystallography ◽  
Insight Into

Protein structural biology came a long way since the determination of the first three-dimensional structure of myoglobin about six decades ago. Across this period, X-ray crystallography was the most important experimental method for gaining atomic-resolution insight into protein structures. However, as the role of dynamics gained importance in the function of proteins, the limitations of X-ray crystallography in not being able to capture dynamics came to the forefront. Computational methods proved to be immensely successful in understanding protein dynamics in solution, and they continue to improve in terms of both the scale and the types of systems that can be studied. In this review, we briefly discuss the limitations of X-ray crystallography in studying protein dynamics, and then provide an overview of different computational methods that are instrumental in understanding the dynamics of proteins and biomacromolecular complexes.

Determining the shape and periodicity of nanostructures using small-angle X-ray scattering

2015 ◽  
Vol 48 (5) ◽  
pp. 1355-1363 ◽  
Author(s):  
Daniel F. Sunday ◽  
Scott List ◽  
Jasmeet S. Chawla ◽  
R. Joseph Kline
Keyword(s):  
Small Angle ◽  
Semiconductor Industry ◽  
Three Dimensional ◽  
Critical Dimension ◽  
Dimensional Structure ◽  
Critical Dimensions ◽  
X Ray ◽  
Line Shapes ◽  
X Ray Scattering ◽  
Ray Scattering

The semiconductor industry is exploring new metrology techniques capable of meeting the future requirement to characterize three-dimensional structure where the critical dimensions are less than 10 nm. X-ray scattering techniques are one candidate owing to the sub-Å wavelengths which are sensitive to internal changes in electron density. Critical-dimension small-angle X-ray scattering (CDSAXS) has been shown to be capable of determining the average shape of a line grating. Here it is used to study a set of line gratings patternedviaa self-aligned multiple patterning process, which resulted in a set of mirrored lines, where the individual line shapes were asymmetric. The spacing between lines was systematically varied by sub-nm shifts. The model used to simulate the scattering was developed in stages of increasing complexity in order to justify the large number of parameters included. Comparisons between the models at different stages of development demonstrate that the measurement can determine differences in line shapes within the superlattice. The shape and spacing between lines within a given set were determined to sub-nm accuracy. This demonstrates the potential for CDSAXS as a high-resolution nanostructure metrology tool.

scholarly journals Structural analysis of tRNA(His) guanylyltransferase comlexed with tRNA

2014 ◽  
Vol 70 (a1) ◽  
pp. C1816-C1816
Author(s):  
Akiyoshi Nakamura ◽  
Taiki Nemoto ◽  
Isao Tanaka ◽  
Min Yao
Keyword(s):  
Crystal Structures ◽  
Domain Architecture ◽  
Gel Filtration ◽  
Three Dimensional ◽  
Trna Synthetase ◽  
Dimensional Structure ◽  
Catalytic Core ◽  
X Ray ◽  
Catalytic Activation ◽  
X Ray Scattering

tRNA(His) guanylyltransferase (Thg1) of eukaryote adds a guanylate to the 5' end of immature or incorrectly processed tRNAs (3'-5' polymerization) by three reaction steps: adenylylation; guanylylation and dephosphorylation. This additional guanylate provides the major identity element for histidyl-tRNA synthetase to recognize its cognate substrate tRNA(His) and differentiates tRNA(His) from the pool of tRNAs present in the cell (1). Previous studies indicate that Thg1 is a structural homolog of canonical 5'-3' polymerases in the catalytic core with no obvious conservation of the amino acid sequence(2). However, the substrate binding of Thg1 is unclear and requires information on the three-dimensional structure in complex with tRNA. In this study, we determined the crystal structures of Thg1 from Candida albicans (CaThg1) in tRNA-bound (CaThg1-tRNA), ATP-bound (CaThg1-ATP), and GTP-bound (CaThg1-GTP) form, and elucidated how Thg1 functions as a reverse polymerase to add nucleotide(3). The crystal structures of CaThg1-tRNA complex shows that two tRNAs are bound to tetrameric Thg1 in parallel orientation which is consistent with SAXS (Small angle X-ray scattering) and gel filtration analysis. One tRNA interacts with three monomers for its positioning, anticodon recognition, and catalytic activation. The end of the acceptor stem and the anticodon loop are both recognized by the same sub-domain belonging to the different monomers. Moreover, the structural comparison of Thg1-tRNA with canonical 5'-3' polymerase shows that the domain architecture of Thg1 is reversed to that of canonical 5'-3' polymerase.

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