Dynamics and Protein–Solvent Interactions of Hemoglobin in T and R Quaternary Conformation | Zendy

Chiara Caronna | Zendy; Antonio Cupane | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Dynamics and Protein–Solvent Interactions of Hemoglobin in T and R Quaternary Conformation

Author(s) -

Chiara Caronna,

Antonio Cupane

Publication year - 2002

Publication title -

journal of spectroscopy

Language(s) - English

Resource type - Journals

eISSN - 2314-4920

pISSN - 2314-4939

DOI - 10.1155/2002/495614

Subject(s) - protein quaternary structure , hemoglobin , solvent , chemistry , quaternary , crystallography , amide , protein dynamics , molecular dynamics , computational chemistry , organic chemistry , biochemistry , biology , paleontology , protein subunit , gene

In this work we report the thermal behaviour of the amide I′ band of carbonmonoxy and deoxy hemoglobin in 65% v/v glycerolD8/D2O solutions and in the temperature interval 10–295 K. Following recent suggestions in the literature, we analyze the amide I′ band in terms of two components, one at about 1630 cm−1 and the other at about 1650 cm−1, that are assigned to solvent‒exposed and buried α‒helical regions, respectively.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research