Elucidating the binding thermodynamics of 8-anilino-1-naphthalene sulfonic acid with the A-state of α-lactalbumin: An isothermal titration calorimetric investigation-Reference-Cited by-同舟云学术

Elucidating the binding thermodynamics of 8-anilino-1-naphthalene sulfonic acid with the A-state of α-lactalbumin: An isothermal titration calorimetric investigation

Published:2006 Issue:3 Volume:83 Page:205-212
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Singh Sreelekha K.,Kishore Nand

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.20547/fullpdf

Reference46 articles.

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3. Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the β1,4-galactosyltransferase-I11Edited by R. Huber

4. Structure and dynamics of the acid-denatured molten globule state of .alpha.-lactalbumin: a two-dimensional NMR study

5. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin

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