Table 1.

Peptides that showed decreased solvent accessibility upon protein–protein complexation

Peptide MH+	Residues	k(complex)*, min−1	No. of Ds slowly exchanging	Surface area protected, Å2
PKA complexed to PKI(5–24)
ATP-binding site
1147.6052	164–172	0.004	1.3	148
1260.6933	163–172	0.028	1.6	148
1373.7837	164–174	0.007	1.4	180
Glycine-rich loop
1194.6463	44–54	0.037	2.4	223
1341.7118	43–54	0.024	2.0	224
1584.8087	41–54	0.014	2.1	224
PKI(5–24)-binding site
1628.8925	133–145	0.016	1.0	80
1708.8816	237–250	0.0016	1.1	179
Thrombin complexed to TMEGF(4–5)
Anion-binding exosite I
2127.2265	96–112	0.36	2.1	NA†
2473.3970	97–116	0.13	3.7	NA
2586.4805	97–117	0.23	3.2	NA
Potential connection to active site
2144.1661	117–132	0.74	2.4	NA
2530.3606	118–136	ND‡	ND	NA

^*The value of the slowed off-exchange rate in the complex k_{(PKA-PKI(5–24)} or k_{(thrombin-TM)} corresponds to the slow ensemble off-exchange rate calculated from the bi-exponential fit of the data (PKA data shown in Fig. 5, thrombin data not shown). 

^†The complex studied here is of TMEGF(4–5) for which a structure is not known. Only the structure of a 19 residue peptide from TM bound to thrombin is known. 

^‡Although the 2530.3606 peak shifted significantly, the signal was weak and quantitative kinetics were not determined.