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Cited by 482

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Structural Basis of the Tanford Transition of Bovine β-Lactoglobulin,

Qin, Bin Y., Bewley, Maria C., Creamer, Lawrence K., Baker, Heather M., Baker, Edward N., Jameson, Geoffrey B.·1998·Biochemistry

Abstract

The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.

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Metadata

Authors
Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, H. M., Baker, E. N., & Jameson, G. B.
Venue
Biochemistry
Published
1998-09-18
Volume
37
Issue
40
Pages
14014-14023
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2031674548
Cited by
482
References
3
FWCI
3.83
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural Basis of the Tanford Transition of Bovine β-Lactoglobulin,. https://app.cochat.ai/papers/10.1021/bi981016t
The paper
Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, H. M., Baker, E. N., & Jameson, G. B. (1998). Structural Basis of the Tanford Transition of Bovine β-Lactoglobulin,. Biochemistry. https://doi.org/10.1021/bi981016t

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