PEPTIDE MODELS .1. TOPOLOGY OF SELECTED PEPTIDE CONFORMATIONAL POTENTIAL-ENERGY SURFACES (GLYCINE AND ALANINE DERIVATIVES)

被引:261
作者
PERCZEL, A
ANGYAN, JG
KAJTAR, M
VIVIANI, W
RIVAIL, JL
MARCOCCIA, JF
CSIZMADIA, IG
机构
[1] UNIV TORONTO, DEPT CHEM, TORONTO M5S 1A1, ONTARIO, CANADA
[2] EOTVOS LORAND UNIV, INST ORGAN CHEM, H-1364 BUDAPEST 5, HUNGARY
[3] UNIV NANCY 1, CHIM THEOR LAB, F-54506 VANDOEUVRE LES NANCY, FRANCE
关键词
D O I
10.1021/ja00016a049
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
N-Formylglycinamide (For-Gly-NH2), N-formyl-L-alaninamide (For-L-Ala-NH2), and N-formyl-D-alaninamide (For-D-Ala-NH2) were subjected to conformational studies by molecular mechanics (MM) and ab initio SCF methods. Both methods predicted the corresponding-gamma (usually labeled as C-7eq) conformations to be the global minimum on the Ramachandran map, E(phi,psi). The number of minima and their approximate location obtained by MM corresponded to those that one might have expected on the basis of multidimensional conformation analysis. However, only the ab initio SCF study was capable of properly describing the effects associated with excessive repulsive or attractive interactions that lead to the annihilation and creation of certain critical points. Consequently, the topology of the MM and SCF conformational potential energy surfaces, E(phi,psi), were found to be remarkably different for the three diamide systems investigated in this work.
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页码:6256 / 6265
页数:10
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