Hydration and activity studies of bovine skeletal muscle proteins and wheat gliadins by nuclear magnetic resonance

"$\sp1$H and $\sp{17}$O NMR studies of water and ion binding to bovine skeletal muscle proteins in solutions and suspensions were carried out as a function of concentration, pH/pD, and salt. Numerical analysis of the data was performed by nonlinear regression on an Apple-MacIntosh II microcomputer, using a thermodynamic linkage approach. The second virial coefficient, B$\sb{\rm o}$, of myosin $A$ and $B$ was obtained from the protein concentration dependence of the relaxation rates at high ionic strength (with 0.5 M NaCl). Myosin self-association in the form of tail-to-tail dimers was inferred from the NMR data in the absence of salt. At higher salt concentrations than 0.6 M NaCl, heptamer formation was inferred for myofibrillar proteins, whereas in the presence of 0.5 M NaCl, myosin was found to be fully dispersed as monomers. The ""binding"" of water to myosin $A$ appears to involve primarily carboxyl groups at high pH and imidazolium or ammonium groups at low pH, with hydration being minimal at the isoelectric point (5.5). The molecular dynamics of hydration water and ions bound to myosin occurred on a time scale of tens of picoseconds. The analysis of $\sp{23}$Na NMR studies of Na$\sp+$ binding to myofibrillar proteins reveals the presence of two types of binding sites on these proteins."

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Food Science

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Mora-Gutierrez, Adela

Contributors dc:contributor

• Baianu, Ion C.

• Agriculture, Food Science and Technology

Statement dc:rights

• Copyright 1989 Mora-Gutierrez, Adela

Language dc:language

eng

Identifier

AAI8924905
(UMI)AAI8924905

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19410