Special Issue "Crystal Structures of Amino Acids and Peptides"

A special issue of Crystals (ISSN 2073-4352).

Deadline for manuscript submissions: closed (15 April 2018)

Special Issue Editor

Guest Editor
Prof. Dr. Carl Henrik Gørbitz

Universitetet i Oslo, Department of Chemistry, Oslo, Norway
Website | E-Mail
Phone: +4722855460
Interests: amino acids; crystal engineering; hydrogen bonding; peptides; phase transitions

Special Issue Information

Dear Colleagues,

Amino acids have a central role in biology as the monomers of a diverse array of proteins vital to life, but also have import functions as isolated molecules or as parts of shorter peptides. Indeed, small peptides find roles ranging from biological signalling molecules and growth factors to construction of porous materials and sensors. The ubiquitous presence and widespread use of amino acids and peptides in nature and in the laboratory hinges on their structures; an understanding of which requires fundamental knowledge of forces and mechanisms governing super-molecular assembly in the solid state and the often minute changes required to push the crystallization outcome in an entirely different direction.

The Special Issue on “Crystal Structures of Various Amino Acids and Peptides” is intended to collect contributions from scientist working with a broad spectrum of crystal properties as well as on crystal growth, manifesting the impact of these small, yet incredibly important molecules. I hope we can inspire each other and open avenues to future research projects into the unknown.

The topics summarized under the keywords cover broadly examples of the greater number of sub-topics in mind and should be seen as examples rather than limitations. Innovative research within chemistry, physics or pharmacy is particularly welcome.

Prof. Dr. Carl Henrik Gørbitz
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Crystals is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Crystal packing at ambient and non-ambient conditions
  • Intermolecular interactions, including hydrogen bonding
  • Energetics and structure prediction
  • Polymorphism and phase transitions
  • Amino acid and peptide co-crystals

Published Papers (2 papers)

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Research

Open AccessArticle The Role of Chirality and Helicity between d- and l-Valine Optical Lattices
Crystals 2018, 8(7), 281; https://doi.org/10.3390/cryst8070281
Received: 23 June 2018 / Accepted: 3 July 2018 / Published: 5 July 2018
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Abstract
With the aim to investigate the role of chirality and helicity between d- and l-valine crystal lattices under Debye temperature 2–20 K, magnetic field dependence of zero-field and 1, 3 and 5 Tesla on the heat capacity were measured. The heat
[...] Read more.
With the aim to investigate the role of chirality and helicity between d- and l-valine crystal lattices under Debye temperature 2–20 K, magnetic field dependence of zero-field and 1, 3 and 5 Tesla on the heat capacity were measured. The heat capacities of d- and l-valine crystals were plotted as Cp vs. T, Cp vs. lnT, Cp/T3 vs. T in the measured temperature. The four Cp/T3 vs. T curves show a split between d- and l-valine from 2 K to 12 K (T << ΘD) which is due to the strength of magnetic fields. It is absent from 12 K to 20 K, which indicates the Schottky anomaly. The Bose–Einstein peak of the (e-p) condensation temperature is 11.20, 11.32, 11.44, 11.46 K for d-valine, and 11.49, 11.59, 11.73, 11.70 K for l-valine, respectively. This finding leads to a zero-field splitting of a broad maximum associated with the Schottky anomaly below the temperature of 12 K which is demonstrated by (e-p) Bose–Einstein condensation through the hydrogen of peptide bond in the alpha helix at zero momentum space onto d- and l-valine optical lattices. Full article
(This article belongs to the Special Issue Crystal Structures of Amino Acids and Peptides)
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Open AccessArticle Structural Basis for the Influence of A1, 5A, and W51W57 Mutations on the Conductivity of the Geobacter sulfurreducens Pili
Crystals 2018, 8(1), 10; https://doi.org/10.3390/cryst8010010
Received: 15 November 2017 / Revised: 18 December 2017 / Accepted: 21 December 2017 / Published: 25 December 2017
PDF Full-text (71714 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The metallic-like conductivity of the Geobacter sulfurreducens pilus and higher conductivity of its mutants reflected that biological synthesis can be utilized to improve the properties of electrically conductive pili. However, the structural basis for diverse conductivities of nanowires remains uncertain. Here, the impacts
[...] Read more.
The metallic-like conductivity of the Geobacter sulfurreducens pilus and higher conductivity of its mutants reflected that biological synthesis can be utilized to improve the properties of electrically conductive pili. However, the structural basis for diverse conductivities of nanowires remains uncertain. Here, the impacts of point mutations on the flexibility and stability of pilins were investigated based on molecular dynamics simulations. Structures of the G. sulfurreducens pilus and its mutants were constructed by Rosetta. Details of the structure (i.e., electrostatic properties, helical parameters, residue interaction network, distances between amino acids, and salt bridges) were analyzed by PDB2PQR, Rosetta, RING, PyMOL, and VMD, respectively. Changes in stability, flexibility, residue interaction, and electrostatic properties of subunits directly caused wild-type pilin and its mutants assemble different structures of G. sulfurreducens pili. By comparing the structures of pili with different conductivities, the mechanism by which the G. sulfurreducens pilus transfers electron along pili was attributed, at least in part, to the density of aromatic rings, the distances between neighboring aromatic rings, and the local electrostatic environment around aromatic contacts. These results provide new insight into the potential for the biological synthesis of highly electrically conductive, nontoxic nanowires. Full article
(This article belongs to the Special Issue Crystal Structures of Amino Acids and Peptides)
Figures

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