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A calorimetric study of pH-dependent thermal unfolding of leghemoglobin a from soybean

โœ Scribed by Rumiana D Tzoneva; Ekaterina I Mishonova-Alexova


Book ID
117047376
Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
205 KB
Volume
1364
Category
Article
ISSN
0005-2728

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A scanning calorimetric study of the the
โœ Julian M. Sturtevant; Marilyn Emerson Holtzer; Alfred Holtzer ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 510 KB

The reversible thermally induced unfolding of various forms of tropomyosin, a two-chain a-helical coiled coil, has been studied by high-sensitivity differential scanning calorimetry (DSC) . Included in the study are the reduced and oxidized (disulfide cross-linked) forms of am-and PP-tropomyosin, an