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Solid-State NMR Analyses Revealed the Structure Dependence of the Molecular Dynamics for ω-Amino Acids.
MedLine Citation:
PMID:  22251439     Owner:  NLM     Status:  Publisher    
Molecular dynamics of metabolites is structure dependent and vitally important for their interactive functions in their potential applications as natural materials. To understand the relationship between molecular structure and dynamics, molecular motions of four structurally related ω-amino acids (β-alanine, γ-aminobutyric acid, 5-aminovaleric acid and 6-aminocaproic acid) were investigated by measuring the proton spin-lattice relaxation times (T1, T1ρ) as a function of temperature (180-440 K). 13C CPMAS NMR and DSC analyses were performed to obtain complimentary information. All these ω-amino acids showed no phase transition in the temperature range studied. They had outstandingly long proton T1 at 300 MHz and even at 20 MHz for the deuterated forms. Molecular dynamics of all these ω-amino acids were dominated by the reorientation motions of amino groups and backbone motions except in β-alanine. The activation energies for amino group reorientations were positively correlated with the strength of hydrogen-bonds involving these groups in the crystals and the carbon-chain lengths whereas such energies for the backbone motions were inversely correlated with the carbon-chain lengths. These findings provided essential information for molecular dynamics of ω-amino acids and demonstrated the combined solid-state NMR methods as a useful approach for understanding the structural dependence of molecular dynamics.
Jing Huang; Limin Zhang; Huiru Tang
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-1-17
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  -     ISSN:  1520-5207     ISO Abbreviation:  -     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-1-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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