Effect of inter-subunit contact on intramolecular conformational motility (conformational stability) 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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G protein-coupled receptors (GPCRs) are activated by ligand binding, allowing extracellular signals to be efficiently transmitted through the membrane to the G protein recognition site, 40 Å away. Utilizing His residues found spaced throughout the GPCR, rhodopsin, we used His hydrogen-deuterium exchange (His-HDX) to monitor long-time scale structural rearrangements previously inaccessible by ot...
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The previously developed theory for treating the kinematics of polymers in dense media (Bahar, I.; Erman, B.; Monnerie, L. Macromolecules 1992, 25, 6309, 6315) is extended to include the influence of internal conformational energy barriers on the mechanism of motion. The method is based on the solution of a constrained equation of motion in the presence of dissipative forces due to friction. Su...
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Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1976
ISSN: 0014-5793
DOI: 10.1016/0014-5793(76)80741-7