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. Author manuscript; available in PMC: 2016 Jun 10.
Published in final edited form as: Biochemistry. 2009 Aug 4;48(30):7219–7228. doi: 10.1021/bi9005557

Table 2.

Fluorescence Quenching Parameters for Palmitic Acid and C12SL Binding to Single Trp Mutants of Human Tear Lipocalina

C12SL
 PA
Trp mutant KSVapp × 10−3
(M−1)		 KD × 10−3
(M−1)		 kq × 10−12
(M−1 s−1)		 KS × 10−3
(M−1)		 KSVapp × 10−3
(M−1)		 KD × 10−3
(M−1)		 kq × 10−12
(M−1 s−1)		 KS × 10−3
(M−1)
W22 36.2 (1.0) 15.4 (1.2) 3.6 17.5 (1.6) 12.9 (0.8) 10.2 (0.7) 2.4 2.1 (1.0)
W24 35.8 (0.3) 13.1 (0.5) 4.0 20.1 (0.8) 3.8 (0.9) 3.8 (0.9) 1.1 0
W25 17.1 (0.9) 10.3 (0.9) 2.3 6.0 (1.2) 2.7 (0.7) 2.7 (0.7) 0.6 0
W26 24.2 (0.8) 7.1 (1.0) 1.8 15.8 (1.4) 3.5 (0.7) 3.5 (0.7) 0.8 0
W27 9.5 (0.9) 9.5 (0.9) 1.7 0 0 0 0 0
W28 51.9 (1.5) 22.3 (1.9) 5.4 24.2 (2.5) 23.1 (2.2) 12.3 (1.9) 3.0 9.8 (2.5)
W30 23.4 (0.6) 8.5 (1.1) 3.3 13.8 (1.6) 0 0 0 0
W33 42.0 (0.9) 11.0 (1.1) 3.6 29.0 (1.9) 0 0 0 0
W34 21.1 (1.2) 4.9 (1.2) 1.5 15.5 (1.2) 7.0 (0.8) 7.0 (0.8) 2.1 0
W35 45.6 (1.1) 12.2 (1.1) 3.0 30.7 (1.6) 0 0 0 0
W36 24.6 (0.6) 13.6 (1.2) 3.3 9.6 (1.1) 0 0 0 0
W37 28.5 (0.6) 19.1 (0.5) 6.3 8.3 (0.7) 20.1 (0.5) 7.6 (0.5) 2.4 11.8 (0.8)
W39 64.9 (1.0) 14.9 (1.2) 3.7 45.1 (1.9) 0 0 0 0
W41 0 0 0 0 0 0 0 0
W49 14.3 (0.3) 7.6 (1.6) 3.1 4.9 (1.8) 5.6 (0.5) 0 0 5.6 (0.5)
W53 8.5 (0.3) 1.1 (0.9) 0.5 7.4 (1.4) 0 0 0 0
W55 28.3 (1.3) 9.6 (2.4) 2.6 17.1 (2.8) 0 0 0 0
W57 27.2 (0.6) 14.7 (1.7) 4.6 10.9 (2.2) 19.5 (0.5) 10.9 (0.5) 3.7 7.8 (0.7)
W59 5.2 (0.5) 5.2 (0.5) 1.6 0 2.8 (0.3) 2.8 (0.3) 0.9 0
W60 11.1 (1.2) 11.1 (1.2) 3.5 0 1.3 (0.5) 1.3 (0.5) 0.4 0
W62 37.7 (0.7) 7.1 (0.6) 2.2 28.6 (0.9) 5.5 (0.6) 5.5 (0.6) 1.7 0
W64 23.4 (0.5) 0 0 23.4 (0.5) 0 0 0 0
W66 17.8 (0.2) 8.8 (1.4) 2.8 8.3 (1.8) 0 0 0 0
W68 17.5 (2.2) 17.5 (2.2) 5.7 0 11.0 (1.8) 11.0 (1.8) 3.5 0
W77 3.2 (0.5) 0 0 3.2 (0.5) 0 0 0 0
W79 21.5 (0.8) 5.2 (1.1) 2.0 15.3 (1.4) 1.1 (0.6) 1.1 (0.6) 0.4 0
W80 7.7 (0.5) 7.7 (0.5) 1.1 0 0 0 0 0
W81 6.9 (0.5) 6.9 (0.5) 1.8 0 0 0 0 0
W82 18.1 (0.4) 2.5 (0.6) 0.8 15.3 (0.9) 0 0 0 0
W84 21.5 (0.8) 3.7 (1.0) 1.5 17.1 (1.5) 2.6 (1.0) 2.6 (1.0) 1.1 0
W86 35.8 (1.0) 9.9 (1.3) 2.5 23.1 (2.4) 1.6 (0.4) 1.6 (0.4) 0.4 0
W88 2.2 (0.3) 6.8 (0.3) 2.1 −4.3 (0.5) −23.0 (1.4) 6.3 (1.3) 1.9 27.0 (1.5)
W97 17.5 (0.9) 6.2 (0.9) 2.4 10.5 (1.3) 31.4 (1.0) 11.6 (1.0) 4.5 17.4 (1.5)
W99 9.5 (0.6) 3.2 (0.6) 1.0 5.9 (0.8) 0 0 0 0
W101 82.4 (3.2) 13.3 (2.4) 3.2 64.7 (3.8) 24.8 (1.5) 33.2 (1.5) 8.0 0
W103 36.2 (1.9) 4.4 (1.2) 1.9 32.1 (2.8) 4.7 (0.3) 4.6 (0.3) 1.7 0
W105 69.9 (1.3) 2.7 (1.2) 1.0 63.8 (2.4) 25.2 (0.3) 4.6 (1.2) 1.9 19.1 1.2)
W106 36.1 (0.8) 12.9 (0.9) 4.0 7.3 (0.6) 6.5 (0.6) 7.3 (0.6) 2.4 0
W107 27.0 (1.4) 5.0 (1.4) 1.0 21.0 (2.1) 10.8 (0.7) 0 0 10.8 (0.7)
W108 −7.3 (0.3) 5.2 (0.5) 1.2 −12.0 (0.6) −12.1 (0.9) 4.1 (0.8) 0.9 19.6 (1.0)
W110 51.5 (1.7) 10.3 (1.2) 3.3 39.2 (1.9) 0 0 0 0
W112 31.6 (1.9) 6.6 (1.5) 2.3 23.0 (2.1) 7.3 (0.9) 2.9 (0.5) 1.0 4.3 (0.9)
W114 59.8 (1.9) 15.8 (1.4) 3.8 37.9 (2.1) 7.6 (0.6) 7.6 (0.6) 1.8 0
W116 6.5 (0.3) 3.3 (0.6) 1.1 2.9 (0.7) 0 0 0 0
a

Errors for quenching parameters are reported as the standard deviation (numbers in parentheses) from the mean value determined from multiple experimental data. Negative numbers reflect increased fluorescence upon ligand binding. KSVapp: apparent Stern-Volmer quenching constant. KD: dynamic