Solvated structure analysis of a conformationally restricted analogue of phenylalanine in a dipeptide model by the AM1-SM2 method

Sándor Lovas; Richard F. Murphy

doi:10.1016/S0166-1280(09)80067-5

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Solvated structure analysis of a conformationally restricted analogue of phenylalanine in a dipeptide model by the AM1-SM2 method

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Solvated structure analysis of a conformationally restricted analogue of phenylalanine in a dipeptide model by the AM1-SM2 method

Sándor Lovas and Richard F. Murphy

Journal of Molecular Structure: THEOCHEM, Vol.311, pp.297-304

311

1994

DOI: https://doi.org/10.1016/S0166-1280(09)80067-5

Abstract

Biochemistry

Condensed Matter Physics

Physical and Theoretical Chemistry

The effects of aqueous solvation on the conformational properties of L- and D-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic) were studied in a model dipeptide by means of AM1 and AM1-SM2 methods. The analysis of calculations predicts equivalent stability of g(−) and g(+) conformations in aqueous phase.

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Title: Solvated structure analysis of a conformationally restricted analogue of phenylalanine in a dipeptide model by the AM1-SM2 method
Creators: Sándor Lovas (Author) - Department of Biomedical Sciences
Richard F. Murphy (Author) - Creighton University
Publication Details: Journal of Molecular Structure: THEOCHEM, Vol.311, pp.297-304
Series: 311
Number of pages: 8
Identifiers: 991005930199002656
Academic Unit: Biomedical Sciences
Language: English
Resource Type: Journal article

Solvated structure analysis of a conformationally restricted analogue of phenylalanine in a dipeptide model by the AM1-SM2 method

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