Theoretical conformational analysis of disulfide-linked tetrapeptides Ac-Cys-Pro-D-Xaa-Cys-NHMe having hydrophobic D-Xaa amino-acid residues

1998 ◽  
Vol 41 (5) ◽  
pp. 623-629 ◽  
Author(s):  
Yuichirou Ishikawa ◽  
Yoshiaki Hirano ◽  
Jun Yoshimoto ◽  
Masahito Oka ◽  
Toshio Hayashi
Keyword(s):  
Amino Acid ◽  
Conformational Analysis ◽  
Amino Acid Residues ◽  
Theoretical Conformational Analysis

scholarly journals Theoretical Conformational Analysis of Disulfide-Linked Tetrapeptides Ac-Cys-Pro-Xaa-Cys-NHMe Having Hydrophobic Xaa Amino-Acid Residues

1998 ◽  
Vol 30 (3) ◽  
pp. 256-261 ◽  
Author(s):  
Yuichirou Ishikawa ◽  
Yoshiaki Hirano ◽  
Jun Yoshimoto ◽  
Masahito Oka ◽  
Toshio Hayashi
Keyword(s):  
Amino Acid ◽  
Conformational Analysis ◽  
Amino Acid Residues ◽  
Theoretical Conformational Analysis

Spatial Structure of the Acth-(6-9)-PGP Molecule

2021 ◽  
Vol 43 (5) ◽  
pp. 500-500
Author(s):  
Namiq Akhmedov Namiq Akhmedov ◽  
Leyla Agayeva Leyla Agayeva ◽  
Gulnara Akverdieva Gulnara Akverdieva ◽  
Rena Abbasli and Larisa Ismailova Rena Abbasli and Larisa Ismailova
Keyword(s):  
Amino Acid ◽  
Spatial Structure ◽  
Main Chain ◽  
Low Energy ◽  
Dihedral Angles ◽  
Amino Acid Residues ◽  
Analysis Method ◽  
Theoretical Conformational Analysis ◽  
Energy Of Hydrogen Bonds ◽  
Low Energy Conformations

The spatial structure of ACTH-(6-9)-PGP molecule has been investigated using theoretical conformational analysis method. Amino acid sequence of the N-terminal pentapeptide fragment of His-Phe-Arg-Trp-Pro of this molecule conforms to the fragment 6-9 of ACTH hormone. Calculations of conformational states of this molecule are carried out regarding nonvalent, electrostatic and torsional interactions and the energy of hydrogen bonds. The spatial structure of the His-Phe-Arg-Trp-Pro-Gly-Pro molecule was estimated on the low–energy conformations of the N-terminal tetrapeptide fragment His-Phe-Arg-Trp and C-terminal tripeptide fragment Pro-Gly-Pro of this molecule. It is shown that the spatial structure of heptapeptide molecule can be presented by 11 low-energy forms of the main chain. The low–energy conformations of this molecule, the values of dihedral angles of the backbone and side chains of the amino acid residues were founded and the energies of intra- and inter-residual interactions were determined.

Conformational analysis of peptides from Cαα-symmetrically disubstituted aromatic α-amino acid residues

Peptides 1990 ◽  
1991 ◽  
pp. 458-459
Author(s):  
C. Toniolo ◽  
M. Crisma ◽  
G. Valle ◽  
G. M. Bonora ◽  
F. Lelj ◽  
...  
Keyword(s):  
Amino Acid ◽  
Conformational Analysis ◽  
Amino Acid Residues

Conformational Analysis of the 20 Naturally Occurring Amino Acid Residues Using ECEPP

1977 ◽  
Vol 10 (1) ◽  
pp. 1-9 ◽  
Author(s):  
S. Scott Zimmerman ◽  
Marcia S. Pottle ◽  
George Némethy ◽  
Harold A. Scheraga
Keyword(s):  
Amino Acid ◽  
Conformational Analysis ◽  
Amino Acid Residues ◽  
Naturally Occurring

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

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