PEPTIDE MODELS .7. THE ENDING OF THE RIGHT-HANDED HELICES IN OLIGOPEPTIDES [FOR-(ALA)(N)-NH2 FOR 2-LESS-THAN-OR-EQUAL-TO-N-LESS-THAN-OR-EQUAL-TO-4] AND IN PROTEINS

被引：23

作者：

PERCZEL, A

ENDREDI, G

MCALLISTER, MA

FARKAS, O

CSASZAR, P

LADIK, J

CSIZMADIA, IG

机构：

[1] EOTVOS LORAND UNIV, INST CHEM, DEPT ORGAN CHEM, BUDAPEST, HUNGARY

[2] UNIV ERLANGEN NURNBERG, INST THEORET CHEM, D-91058 ERLANGEN, GERMANY

[3] UNIV ERLANGEN NURNBERG, LAB NATL FDN CANC RES, D-91058 ERLANGEN, GERMANY

[4] APOTEX INC, TORONTO, ON, CANADA

来源：

JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM | 1995年 / 331卷 / 1-2期

基金：

匈牙利科学研究基金会; 加拿大自然科学与工程研究理事会;

关键词：

D O I：

10.1016/0166-1280(94)03972-N

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The right-handed helical conformation (denoted as alpha(L)) of a single amino-acid diamide (e.g. HCO-NHCHCH3CO-NH2) is not a minimum energy conformation on the ab initio potential energy surface. Computations performed on oligopeptides [For-(Ala)(n)-NH2, for n less than or equal to 4], revealed that the helix-like conformations do exist if the backbone conformation at the carboxyl-end is of delta L type; i.e. (alpha(L))(n-1)delta(L). This suggests that according to SCF computations, the isolated helices end in a type I beta-turn (alpha(L) beta(L)).

引用

页码：5 / 10

页数：6

共 28 条

[1]

Abola EE, 1987, DATA COMMISSION INT, P107

[2]

BENEDETTI E, 1988, PEPTIDES, P465

[3] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].