Two Different Packing Arrangements of Antiparallel Polyalanine

Asakura, Tetsuo; Okonogi, Michi; Horiguchi, Kumiko; Aoki, Akihiro; Saitô, Hazime; Knight, David P.; Williamson, Michael P.

doi:10.1002/anie.201105356

Cited by 44 publications

(194 citation statements)

References 29 publications

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“…The relative intensity between 1 H NH and 1 H α gives quantitative measurement of P‐ and AP‐ arrangement (Figure (E)). It is worth to note that, as reported previously, the short length of Ala 3 and Ala 4 can be crystallized in both P‐ and AP‐β‐sheet structures depending on the solvent treatment whereas the longer alanines form only AP‐structures ,…”

Section: Resultssupporting

confidence: 73%

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

2018

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The beta (β)-sheet structures of oligopeptides and polypeptides can be formed in anti-parallel (AP) and parallel (P) forms, which is an important feature to understand such structures. In principle, P- and AP-β-sheet structures can be identified by the presence (AP) or absence (P) of inter-strand H / H correlations on a diagonal in the corresponding 2D H double quantum (DQ)/ H single quantum (SQ) spectrum due to the different inter-strand H / H distances between the two arrangements. However, the H / H peaks overlap with the H / H peaks, which always give cross-peaks regardless of the β-sheet arrangement. The H / H peaks disturb the observation of the presence/absence of H / H correlations and the assignment of H and H is not always available. Here, 3D N/ H DQ/ H SQ correlation solid-state NMR experiments at fast magic angle spinning (70 kHz) are introduced to distinguish AP- and P-β-sheet structures. The N dimension allows the distinction of H / H peaks from H / H peaks with clear assignments of H and H . In addition, the high natural abundance of H and N enables 3D N/ H DQ/ H SQ experiments of oligo-alanines (Ala ) in four hours without isotope labelling.

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Section: Resultssupporting

confidence: 73%

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

2018

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“…The optimazation of 1 H geometry in the crystal structure of Ala 4 AP b structure resulted in a good fit between experimental and calculated chemical shits of 13 C and 15 N. The structure was compared with the crystal structures of Ala 3 and also the fiber structure of polyalanine with AP b-structure.…”

Section: Resultsmentioning

confidence: 92%

“…13 C, and (c) 15 N. (X-ray: calculated based on single crystal X-ray structure and Opt: 1 H geometry optimized structure). 13 C, and (c) 15 N. (X-ray: calculated based on single crystal X-ray structure and Opt: 1 H geometry optimized structure).…”

Section: Resultsmentioning

confidence: 99%

“…13 The crystal size was small, 100 3 200 3 30 lm 3 , but enough for X-ray diffraction analysis with Spring 8 in Japan. 13 The crystal size was small, 100 3 200 3 30 lm 3 , but enough for X-ray diffraction analysis with Spring 8 in Japan.…”

Section: Overviews Of the Crystal Structure Of Alamentioning

confidence: 99%

“…It is worth to mention that over 10 ppm difference in 13 C chemical shifts between Opt and X-ray were observed for Cb and C@O at about 20 ppm and 170-180 ppm, respectively. It is worth to mention that over 10 ppm difference in 13 C chemical shifts between Opt and X-ray were observed for Cb and C@O at about 20 ppm and 170-180 ppm, respectively.…”

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confidence: 98%

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Difference in the structures of alanine tri‐ and tetra‐peptides with antiparallel β‐sheet assessed by X‐ray diffraction, solid‐state NMR and chemical shift calculations by GIPAW

et al. 2013

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Alanine oligomers provide a key structure for silk fibers from spider and wild silkworms.We report on structural analysis of L-alanyl-L-alanyl-L-alanyl-L-alanine (Ala)4 with anti-parallel (AP) β-structures using X-ray and solid-state NMR. All of the Ala residues in the (Ala)4 are in equivalent positions, whereas for alanine trimer (Ala)3 there are two alternative locations in a unit cell as reported previously (Fawcett and Camerman, Acta Cryst., 1975, 31, 658-665). (Ala)4 with AP β-structure is more stable than AP-(Ala)3 due to formation of the stronger hydrogen bonds. The intermolecular structure of (Ala)4 is also different from polyalanine fiber structure, indicating that the interchain arrangement of AP β-structure changes with increasing alanine sequencelength. Furthermore the precise (1)H positions, which are usually inaccesible by X-ray diffraction method, are determined by high resolution (1)H solid state NMR combined with the chemical shift calculations by the gauge-including projector augmented wave method.

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Silk

Asakura

Kametani

Suzuki

2018

Encyclopedia of Polymer Science and Technology

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Silks are naturally spun fibrous proteins most often associated with silkworms and spiders. For more than 5000 years, silk fiber from Bombyx mori silkworm has been used by mankind as an excellent textile fiber “queen of textiles.” Silk fibers possess excellent mechanical properties due to a combination of strength and extensibility, biocompatibility, and biodegradability. Thus, silks are of high interest for researchers in many fields. Here, we review the current understandings of the production, structures, processing, and properties of silkworms and spider silks. In vivo and in vitro findings in the field of silk research are the basis for the design of new proteins and processing strategies, which will enable applications of these fascinating protein‐based materials in the fields of biomedicine and materials engineering.

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Two Different Packing Arrangements of Antiparallel Polyalanine

Cited by 44 publications

References 29 publications

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

Difference in the structures of alanine tri‐ and tetra‐peptides with antiparallel β‐sheet assessed by X‐ray diffraction, solid‐state NMR and chemical shift calculations by GIPAW

Silk

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Two Different Packing Arrangements of Antiparallel Polyalanine

Cited by 44 publications

References 29 publications

3D 14N/1H Double Quantum/1H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

3D 14N/1H Double Quantum/1H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

Difference in the structures of alanine tri‐ and tetra‐peptides with antiparallel β‐sheet assessed by X‐ray diffraction, solid‐state NMR and chemical shift calculations by GIPAW

Silk

Contact Info

Product

Resources

About

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance

3D ¹⁴N/¹H Double Quantum/¹H Single Quantum Correlation Solid‐State NMR for Probing the Parallel and Anti‐Parallel Beta‐Sheet Arrangement of Oligo‐Peptides at Natural Abundance