Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange
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چکیده
منابع مشابه
Conformational stability of ribonuclease T1 determined by hydrogen-deuterium exchange.
The hydrogen-deuterium exchange kinetics of 37 backbone amide residues in RNase T1 have been monitored at 25, 40, 45, and 50 degrees C at pD 5.6 and at 40 and 45 degrees C at pD 6.6. The hydrogen exchange rate constants of the hydrogen-bonded residues varied over eight orders of magnitude at 25 degrees C with 13 residues showing exchange rates consistent with exchange occurring as a result of g...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1977
ISSN: 0014-5793
DOI: 10.1016/0014-5793(77)80202-0