Structural investigations into the avian MHC-I like protein YF1*7.1

Structural investigations of biological macromolecules commonly employ CTEM with negative staining techniques. Difficulties in valid image interpretation arise, however, due to problems such as variability in thickness and degree of penetration of the staining agent, noise from the supporting film, and artifacts from defocus phase contrast effects. In order to determine the effects of these variables on biological structure, as seen by the electron microscope, negative stained macromolecules of high density lipoprotein-3 (HDL3) from human serum were analyzed with both CTEM and STEM, and results were then compared with CTEM micrographs of freeze-etched HDL3. In addition, we altered the structure of this molecule by digesting away its phospholipid component with phospholipase A2 and look for consistent changes in structure.

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A tilting high temperature gas reaction chamber for the JEM 7A T.E.M.

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100107496 ◽

1978 ◽

Vol 36 (1) ◽

pp. 70-71

Author(s):

Brian L. Rhoades

Keyword(s):

Cross Section ◽

Reaction Chamber ◽

Objective Lens ◽

Reduced Cross Section ◽

Cross Sectional ◽

Structural Investigations ◽

Transmission Electron ◽

Dynamic Experiments ◽

Successful Design ◽

Thermocouple Junction

A gas reaction chamber has been designed and constructed for the JEM 7A transmission electron microscope which is based on a notably successful design by Hashimoto et. al. but which provides specimen tilting facilities of ± 15° aboutany axis in the plane of the specimen.It has been difficult to provide tilting facilities on environmental chambers for 100 kV microscopes owing to the fundamental lack of available space within the objective lens and the scope of structural investigations possible during dynamic experiments has been limited with previous specimen chambers not possessing this facility.A cross sectional diagram of the specimen chamber is shown in figure 1. The specimen is placed on a platinum ribbon which is mounted on a mica ring of the type shown in figure 2. The ribbon is heated by direct current, and a thermocouple junction spot welded to the section of the ribbon of reduced cross section enables temperature measurement at the point where localised heating occurs.

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Structural investigations of polytypes in Zn1−xMgxSe by transmission electron microscopy and cathodoluminescence

Journal of Crystal Growth ◽

10.1016/s0022-0248(97)00787-2 ◽

1998 ◽

Vol 184-185 (1-2) ◽

pp. 1015-1020

Author(s):

J Lenzner

Keyword(s):

Electron Microscopy ◽

Transmission Electron Microscopy ◽

Structural Investigations ◽

Transmission Electron

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Cloning, expression and structural investigations of P5βR-like enone reductases from various

Planta Medica ◽

10.1055/s-0030-1265866 ◽

2010 ◽

Vol 76 (12) ◽

Author(s):

P Bauer ◽

M Brydziun ◽

F Müller-Uri ◽

W Kreis

Keyword(s):

Structural Investigations

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Structural investigations of two bifunctional co-dependent enzymes, MtmGIV and MtmC, involved in the biosynthesis of mithramycin

Planta Medica ◽

10.1055/s-0034-1382745 ◽

2014 ◽

Vol 80 (10) ◽

Author(s):

JM Chen ◽

C Hou ◽

OV Tsodikov ◽

J Rohr

Keyword(s):

Structural Investigations

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Ligand Design for Specific MHC Class I Molecules on the Cell Surface

10.26434/chemrxiv.12865688 ◽

2020 ◽

Author(s):

Xizheng Sun ◽

Reika Tokunaga ◽

Yoko Nagai ◽

Ryo Miyahara ◽

Akihiro Kishimura ◽

...

Keyword(s):

Cell Surface ◽

Mhc Class I ◽

Targeted Delivery ◽

Peptide Ligands ◽

Class I ◽

Class I Mhc ◽

Mhc I ◽

Histocompatibility Complex ◽

High Binding Affinity ◽

Mhc Class I Molecules

<p><a></a><a></a><a>We have validated that ligand peptides designed from antigen peptides could be used for targeting specific major histocompatibility complex class I (MHC-I)</a> molecules on cell surface. To design the ligand peptides, we used reported antigen peptides for each MHC-I molecule with high binding affinity. From the crystal structure of the peptide/MHC-I complexes, we determined a modifiable residue in the antigen peptides and replaced this residue with a lysine with an ε-amine group modified with functional molecules. The designed ligand peptides successfully bound to cells expressing the corresponding MHC-I molecules via exchange of peptides bound to the MHC-I. We demonstrated that the peptide ligands could be used to transport a protein or a liposome to cells expressing the corresponding MHC-I. The present strategy may be useful for targeted delivery to cells overexpressing MHC-I, which have been observed autoimmune diseases.</p>

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