Molecular Modeling of Globular Proteins : Strategy 1D ⇒ 3D: Secondary Structures and Epitopes

1997 ◽  
pp. 121-150 ◽  
Author(s):  
Alain J. P. Alix
Keyword(s):  
Molecular Modeling ◽  
Secondary Structures ◽  
Globular Proteins

Design, synthesis, and conformational analysis of 3-cyclo-butylcarbamoyl hydantoins as novel hydrogen bond driven universal peptidomimetics

2018 ◽  
Vol 16 (4) ◽  
pp. 521-525 ◽  
Author(s):  
M. C. Bellucci ◽  
M. Frigerio ◽  
C. Castellano ◽  
F. Meneghetti ◽  
A. Sacchetti ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Molecular Modeling ◽  
Conformational Analysis ◽  
Secondary Structures ◽  
Nmr Studies ◽  
Design Synthesis ◽  
X Ray ◽  
Α Helix

3-cyclo-Butylcarbamoyl hydantoins are able to mimic α-helix and β-turn secondary structures as assessed by molecular modeling, NMR studies, and X-ray analysis.

Formation and stability of secondary structures in globular proteins

1993 ◽  
Vol 3 (2) ◽  
pp. 245-253 ◽  
Author(s):  
J. Bascle ◽  
T. Garel ◽  
H. Orland
Keyword(s):  
Secondary Structures ◽  
Globular Proteins

Second Derivative near Infrared Studies on the Structural Characterisation of Proteins

1998 ◽  
Vol 6 (A) ◽  
pp. A253-A257 ◽  
Author(s):  
Mitsuhiro Miyazawa ◽  
Masashi Sonoyama
Keyword(s):  
Near Infrared ◽  
Nir Spectroscopy ◽  
Secondary Structures ◽  
Globular Proteins ◽  
The Other ◽  
Second Derivative ◽  
Structural Characterisation ◽  
Sheet Structure ◽  
Infrared Studies ◽  
Characteristic Component

Fourier Tranform near infrared (FT-NIR) spectra have been measured for several globular proteins which vary widely in the relative amounts of different secondary structures. In order to assist in the interpretation of the NIR spectra in the region between 5000 and 4000 cm−1, FT-NIR measurements of silk fibroin with different secondary structures were also carried out. The second derivative procedures showed that the broad contour near 4610 cm−1 consists of several overlapping components and each relative intensity is significantly changed with the proteins. In particular, the band near 4525 cm−1 seemed to be a characteristic component of sheet structure. On the other hand, low-wavenumber NIR bands in 4500– 4000 cm−1 region were considered to reflect the amino acid compositions of proteins. These experimental data suggested that NIR spectroscopy can be used for structural analyses and characterisations of proteins.

Albumins as Embedding Media for Electron Microscopy

1969 ◽  
Vol 27 ◽  
pp. 422-423 ◽  
Author(s):  
J. L. Farrant ◽  
J. D. McLean
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
High Temperature ◽  
Biological Material ◽  
Globular Proteins ◽  
The Past ◽  
Antibody Staining ◽  
Thin Sectioning ◽  
Embedding Medium

For electron microscope techniques such as ferritin-labeled antibody staining it would be advantageous to have available a simple means of thin sectioning biological material without subjecting it to lipid solvents, impregnation with plastic monomers and their subsequent polymerization. With this aim in view we have re-examined the use of protein as an embedding medium. Gelatin which has been used in the past is not very satisfactory both because of its fibrous nature and the high temperature necessary to keep its solutions fluid. We have found that globular proteins such as the serum and egg albumins can be cross-linked so as to yield blocks which are suitable for ultrathin sectioning.

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