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. 2009 Jul 19;45(1-2):121–131. doi: 10.1007/s10858-009-9342-y

Fig. 4.

Fig. 4

a Difference in 15N chemical shifts for all-Ala α-LA at 6 and 10 M urea at 20°C [δ15N(10 M)–δ15N(6 M)]. b–e Experimental RDCs recorded for all-Ala α-LA in compressed polyacrylamide gels at 20°C (black) are compared with predicted RDCs for all-Ala α-LA based on a coil-model (red). Measurements were made in b 4 M, c 6 M, d 8 M and e 10 M urea. The secondary structure and domain organization found in native α-lactalbumin is summarized above