Table 4.

Changes in % Deuteration for Peptide and Protein Binding to IIa at 1 and 10 Minutes Relative to Free IIa pH 6.5^a

	20:1				40:1		1.6:1
	Hirudin		GpIbα		γ′		GpIbα 3S		GpIbα 2S
Residues	1 m	10 m	1 m	10 m	1 m	10 m	1 m	10 m	1 m	10 m
−13 to −4	−3.5	1.2	−12.8	−3.2	−15.8	−7.6	−14.8	−5.4	−8.5	−1.2
46–52	−0.2	0.3	0.0	−0.6	−0.3	−0.6	−0.2	−0.6	−1.4	−0.3
65–84	−24.9b	−18.6	−15.6	−4.3	−19.9	−8.9	−13.2	−3.9	−7.7	−2.7
85–99	−3.6	2.0	−13.7	−12.1	−13.1	−10.2	−13.0	−10.3	−8.0	−7.2
106–113	−5.8	0.1	−8.4	−7.0	−7.9	−6.1	n/a	n/a	n/a	n/a
106–116	−4.1	−0.3	−6.7	−6.6	−6.2	−5.6	−2.6	−3.6	−2.6	−2.6
135–149D	−5.0	−7.1	−5.5	−3.6	n/a	n/a	−4.8	−4.4	−4.8	−4.8
173–180	−5.1	−2.2	−5.4	−11.9	−7.8	−11.5	n/a	n/a	n/a	n/a
173–181	−1.6	−1.1	−5.5	−14.0	−8.4	−13.0	−7.0	−11.6	−7.0	−10.6
202–207	−1.0	−1.2	−4.7	−1.9	−7.6	−2.5	n/a	n/a	n/a	n/a

^aThe % change for a particular peptide is calculated as described in (38)

^bThe values in bold represent significant changes in deuteration of greater than −4.5%.