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The conformational propensities of unfolded states of apomyoglobin have been investigated by measurement of residual dipolar couplings between 15 N and 1 H in backbone amide groups. Weak alignment of apomyoglobin in acid and urea-unfolded states was induced with both stretched and compressed polyacrylamide gels. In 8 M urea solution at pH 2.3, conditions under which apomyoglobin...
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