Met-Cars: mass deposition and preliminary structural study via TEM

Gao, Lin; Lyn, Margaret E.; Bergeron, Denis E.; Castleman, A. W.

doi:10.1016/s1387-3806(03)00250-1

Cited by 25 publications

(24 citation statements)

References 38 publications

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“…As a result, clusters AlB À 8 and Al 2 B À 7 can be selected as candidates of novel nanomaterials. For example, they can be deposited on substrate via soft landing or be inserted into a carbon nanotube to form peapods such as Na 6 Pb [55,56]. …”

Section: Homo-lumo Gaps and Charge Transfermentioning

confidence: 99%

Probing the structural and electronic properties of boron cluster anions doped with one or two aluminum atoms

Wang

Chen

et al. 2014

Computational and Theoretical Chemistry

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Section: Homo-lumo Gaps and Charge Transfermentioning

confidence: 99%

Probing the structural and electronic properties of boron cluster anions doped with one or two aluminum atoms

Wang

Chen

et al. 2014

Computational and Theoretical Chemistry

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“…For example, it can be deposited on substrate via soft landing or be inserted into a carbon nanotube to form peapods such as Na 6 Pb. 42,43 It needs to be mentioned that Luo et al investigated the MB n ͑M = Cr, Mn, Fe, Co, Ni, n =1-7͒ clusters using DFT method in a recent paper. 32 The average binding energies of the FeB n ͑n =1-7͒ clusters obtained in their work are also plotted in Fig.…”

Section: B Binding Energymentioning

confidence: 99%

Structures and electronic properties of small FeBn (n=1–10) clusters

Yang

Xiong

2008

The Journal of Chemical Physics

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The geometries, stabilities, electronic properties, and magnetism of FeB(n) clusters up to n=10 are systematically studied with density functional theory. We find that our optimized structures of FeB(2), FeB(3), FeB(4), and FeB(5) clusters are more stable than those proposed in previous literature. The results show that it is favorable for the Fe atom to locate at the surface, not at the center of the cluster, and that FeB(4) and FeB(9) clusters exhibit high stability. For all the FeB(n) clusters studied, we find the charge transfer from Fe to B site and the coexistence of ionic and covalent bonding characteristics. The computed total magnetic moments of the lowest-energy structures oscillate with the cluster size and are quenched at n=4, 6, 8, and 10.

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“…Preparation of directionally aligned ahelical peptide layers on substrates has attracted significant attention because the resulting strong net dipole is useful for a variety of applications in photonics, [2,3] molecular electronics, [4] and catalysis. Existing technologies for the production of a-helical peptide surfaces are based on a variety of solution-phase synthetic strategies [2,5,8] that usually require relatively large quantities of purified materials.Preparative mass spectrometry based on soft landing (SL) [9][10][11][12][13][14][15][16][17][18] of mass-selected ions is a viable alternative to the existing surface modification approaches. Existing technologies for the production of a-helical peptide surfaces are based on a variety of solution-phase synthetic strategies [2,5,8] that usually require relatively large quantities of purified materials.…”

mentioning

confidence: 99%

Helical Peptide Arrays on Self‐Assembled Monolayer Surfaces through Soft and Reactive Landing of Mass‐Selected Ions

Wang

Laskin

2008

Angew Chem Int Ed

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The a helix, a common building block of the protein secondary structure, plays an important role in determining protein structure and function. The biological function of the a helix is mainly attributed to its large macrodipole [1] originating from the alignment of individual dipole moments of peptide bonds. Preparation of directionally aligned ahelical peptide layers on substrates has attracted significant attention because the resulting strong net dipole is useful for a variety of applications in photonics, [2,3] molecular electronics, [4] and catalysis. [5][6][7] In addition, conformationally-selected a-helical peptide arrays can be used for detailed characterization of molecular recognition steps critical for protein folding, enzyme function, and DNA binding by proteins. Existing technologies for the production of a-helical peptide surfaces are based on a variety of solution-phase synthetic strategies [2,5,8] that usually require relatively large quantities of purified materials.Preparative mass spectrometry based on soft landing (SL) [9][10][11][12][13][14][15][16][17][18] of mass-selected ions is a viable alternative to the existing surface modification approaches. It has been demonstrated that SL enables highly specific preparation of uniform thin films of biological molecules on substrates. [19][20][21] In addition, reactive landing (RL), in which SL is followed by covalent linking of molecules to chemically reactive surfaces, can be used for controlled immobilization of peptides and proteins on solid supports. [22,23] Because SL is a relatively gentle ion deposition technique, it is easy to preserve the primary structure of deposited species. However, it is very difficult to control the secondary structure of soft-landed biomolecules, because electrospray ionization (ESI) utilized in these experiments generates ions in a variety of different conformations. Previous studies reported retention of the secondary and possibly tertiary structure by soft-landed proteins. [19a, 21, 22] Herein, we demonstrate that SL can be used to prepare peptides on substrates in stable conformations that do not exist in solution.This study focuses on the preparation of conformationally-selected peptide arrays using SL of mass selected peptide ions on self-assembled monolayer (SAM) surfaces. The singly protonated Ac-A 15 K peptide was selected as a model system for this study because ion mobility measurements and molecular dynamics (MD) simulations demonstrated that this peptide forms a very stable a-helical conformation in the gas phase, which is stabilized by the interaction between the protonated C-terminal lysine residue and the dipole of the helix.[24] Formation of the a-helical peptide array is demonstrated on an inert SAM of alkylthiol on gold (HSAM) and covalent immobilization of the Ac-A 15 K peptide on a reactive SAM of N-hydroxysuccinimidyl ester terminated alkylthiol on gold (NHS-SAM) with retention of the secondary structure. Because the NHS-SAM surface readily reacts with primary amino groups in proteins or pepti...

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Met-Cars: mass deposition and preliminary structural study via TEM

Cited by 25 publications

References 38 publications

Probing the structural and electronic properties of boron cluster anions doped with one or two aluminum atoms

Probing the structural and electronic properties of boron cluster anions doped with one or two aluminum atoms

Structures and electronic properties of small FeBn (n=1–10) clusters

Helical Peptide Arrays on Self‐Assembled Monolayer Surfaces through Soft and Reactive Landing of Mass‐Selected Ions

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