Side-chain Conformational Thermodynamics of Aspartic Acid Residue in the Peptides and Achatin-I in Aqueous Solution

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2004 Jan 30

PMID 14747347

Citations 1

Authors

Tomohiro Kimura

Nobuyuki Matubayasi

Masaru Nakahara

Affiliations

Soon will be listed here.

Abstract

Sequence-position dependence of the side-chain conformational equilibrium of aspartic acid (Asp) residue is investigated for both model Asp peptides (di- to tetra-) and neuropeptide achatin-I (Gly--Phe-Ala-Asp) in aqueous solution. The trans-to-gauche conformational changes on the dihedral angle of C-C(alpha)-C(beta)-C are analyzed in terms of the standard free energy DeltaG(0), enthalpy DeltaH(0), and entropy -TDeltaS(0). The thermodynamic quantities are obtained by measuring the dihedral-angle-dependent vicinal (1)H-(1)H coupling constants in nuclear magnetic resonance over a wide temperature range. When the carboxyl groups of Asp are ionized, DeltaG(0) in the aqueous phase depends by approximately 1-2 kJ mol(-1) on the sequence position, whereas the energy change in the gas phase (absence of solvent) depends by tens of kJ mol(-1). Therefore, the weak position dependence of DeltaG(0) is a result of the compensation for the intramolecular effect by the hydration (= DeltaG(0)-). The DeltaH(0) and -TDeltaS(0) components, on the other hand, exhibit a notable trend at the C-terminus. The C-terminal DeltaH(0) is larger than the N- and nonterminal DeltaH(0) values due to the intramolecular repulsion between alpha- and beta-. The C-terminal -TDeltaS(0) is negative and larger in magnitude than the others, and an attractive solute-solvent interaction at the C-terminus serves as a structure breaker of the water solvent.

Citing Articles

NMR study on the binding of neuropeptide achatin-I to phospholipid bilayer: the equilibrium, location, and peptide conformation.

Kimura T, Okamura E, Matubayasi N, Asami K, Nakahara M Biophys J. 2004; 87(1):375-85.

PMID: 15240472 PMC: 1304359. DOI: 10.1529/biophysj.103.038950.

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