𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Hydrophobic core of molten-globule state of bovine carbonic anhydrase B

✍ Scribed by Shigeki Mitaku; Sayoko Ishido; Yoshimi Hirano; Hiroyasu Itoh; Ryoichi Kataoka; Nobuhiko Saitô

Publisher
Elsevier Science
Year
1991
Tongue
English
Weight
444 KB
Volume
40
Category
Article
ISSN
0301-4622

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Denaturation of cobalt–carbonic anhydras
Denaturation of cobalt–carbonic anhydrase B from bovine erythrocyte
✍ Leslie F. McCoy Jr.; Kin-Ping Wong 📂 Article 📅 1979 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 703 KB

## Abstract We have attempted to elucidate the mechanism of the acquisition of active‐site conformation in enzymes by studying the unfolding and refolding of Co(II) carbonic anhydrase. This enzyme possesses characteristic absorption and CD spectra in the visible region, which reflect primarily the

Hydrophobic dye inhibits aggregation of
Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding
✍ Bishwajit Kundu; Purnananda Guptasarma 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 200 KB

Association-seeking surfaces on partially structured polypeptides can participate in interactions that are either intramolecular (folding related) or intermolecular (aggregative). During heat shock, intermolecular associations leading to aggregation are prevented through the binding of such surfaces

Study of the “molten globule” intermedia
Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe
✍ G. V. Semisotnov; N. A. Rodionova; O. I. Razgulyaev; V. N. Uversky; A. F. Gripas 📂 Article 📅 1991 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 772 KB

of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR ## SYNOPSIS Binding of the hydrophobic fluorescent probe, 1-anilino-naphthalene-8-sulfonate ( ANS) , to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a mu

1,1,1,3,3,3-hexafluoroisopropanol induce
1,1,1,3,3,3-hexafluoroisopropanol induced thermal unfolding and molten globule state of bovine α-lactalbumin: Calorimetric and spectroscopic studies
✍ Agnita Kundu; Nand Kishore 📂 Article 📅 2004 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 204 KB

## Abstract The thermal denaturation of α‐lactalbumin was studied at pH 7.0 and 9.0 in aqueous 1,1,1,3,3,3‐hexafluoroisopropanol (HFIP) by high‐sensitivity differential scanning calorimetry. The conformation of the protein was analyzed by a combination of fluorescence and circular dichroism measure

Noncooperative temperature melting of a
Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B
✍ E. V. Brazhnikov; Yu. N. Chirgadze; D. A. Dolgikh; O. B. Ptitsyn 📂 Article 📅 1985 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 493 KB

Heat denaturation of native globular proteins is a cooperative process usually connected with the melting of the main part of their regular secondary structure. In this paper, a noncooperative temperature-induced melting of the regular secondary structure in the carbonic anhydrase B at pH 2.6 in hea