1H-Nuclear Magnetic Resonance Studies on the Conformational Changes Related to the Foaming Properties of β-Lactoglobulin-Reference-Cited by-同舟云学术

1H-Nuclear Magnetic Resonance Studies on the Conformational Changes Related to the Foaming Properties of β-Lactoglobulin

Published:1998-10 Issue:10 Volume:81 Page:2580-2587
ISSN:0022-0302
Container-title:Journal of Dairy Science
language:en
Short-container-title:Journal of Dairy Science

Author:

Belloque J.,Smith Gary M.

Publisher

American Dairy Science Association

Subject

Genetics,Animal Science and Zoology,Food Science

Reference36 articles.

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2. Belloque, J. 1996. 1H-FT-NMR studies on the structure stability of the bovine milk whey protein b-lactoglobulin. Ph.D. Diss., Univ. California, Davis.

3. Thermal denaturation of β-lactoglobulin. A 1H NMR study;Belloque;J. Agric. Food Chem.,1998

4. Local secondary structure in ribonuclease A denatured by guanidine HCl near 1°C;Bierzynski;J. Mol. Biol.,1982

5. Bovine β-lactoglobulin at 1.8 Å resolution—still an enigmatic lipocalin;Brownlow;Structure (Lond.),1997

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