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Principles of Fluorescence Spectroscopy

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602 TIME-RESOLVED PROTEIN FLUORESCENCE<br />

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Phys Chem B 108:3879–3889.<br />

44. Tanaka F, Tamai N, Mataga N, Tonomura B, Hiromi K. 1994.<br />

Analysis <strong>of</strong> internal motion <strong>of</strong> single tryptophan in Streptomyces<br />

subtilisin inhibitor from its picosecond time-resolved fluorescence.<br />

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protein dynamics. Biochemistry 16:5546–5551.<br />

52. Eftink MR, Hagaman KA. 1986. The viscosity dependence <strong>of</strong> the<br />

acrylamide quenching <strong>of</strong> the buried tryptophan residue in parvalbumin<br />

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53. Longworth JW. 1968. Excited state interactions in macromolecules.<br />

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55. Gryczynski I, Eftink M, Lakowicz JR. 1988. Conformation heterogeneity<br />

in proteins as an origin <strong>of</strong> heterogeneous fluorescence<br />

decays, illustrated by native and denatured ribonuclease T 1 . Biochim<br />

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56. Eftink MR, Ghiron CA. 1987. Frequency domain measurements <strong>of</strong><br />

the fluorescence lifetime <strong>of</strong> ribonuclease T 1 . Biophys J 52:467–473.<br />

57. Chen LX-Q, Longworth JW, Fleming GR. 1987. Picosecond timeresolved<br />

fluorescence <strong>of</strong> ribonuclease T 1 . Biophys J 51:865–873.<br />

58. Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA. 1993.<br />

Rat annexin V crystal structure: Ca 2+ –induced conformational<br />

changes. Science 261:1321-1324.<br />

59. Sopkova J, Gallay J, Vincent M, Pancoska P, Lewit-Bentley A. 1994.<br />

The dynamic behavior <strong>of</strong> Annexin V as a function <strong>of</strong> calcium ion<br />

binding: a circular dichroism, UV absorption, and steady state and<br />

time-resolved fluorescence study. Biochemistry 33(15):4490–4499.<br />

60. Sopkova J, Vincent M, Takahashi M, Lewit-Bentley A, Gallay J.<br />

1998. Conformational flexibility <strong>of</strong> domain III <strong>of</strong> annexin V studied<br />

by fluorescence <strong>of</strong> tryptophan 187 and circular dichroism: the effect<br />

<strong>of</strong> pH. Biochemistry 37:11962–11970.<br />

61. Toptygin D, Savtchenko RS, Meadow ND, Brand L. 2001.<br />

Homogeneous spectrally- and time-resolved fluorescence emission<br />

from single-tryptophan mutants <strong>of</strong> IIA Glc protein. J Phys Chem B<br />

105:2043–2055.<br />

62. Gryczynski I, Lakowicz JR. Unpublished observations.<br />

63. Nishimoto E, Yamashita S, Szabo AG, Imoto T. 1998. Internal<br />

motion <strong>of</strong> lysozyme studied by time-resolved fluorescence depolarization<br />

<strong>of</strong> tryptophan residues. Biochemistry 37:5599–5607.<br />

64. Poveda JA, Prieto M, Encinar JA, Gonzalez-Ros JM, Mateo CR.<br />

2003. Intrinsic tyrosine fluorescence as a tool to study the interaction<br />

<strong>of</strong> the shaker B "ball" peptide with anionic membranes. Biochemistry<br />

42:7124–7132.<br />

65. Damberg P, Jarvet J, Allard P, Mets U, Rigler R, Gräslund A. 2002.<br />

13 C– 1 H NMR relaxation and fluorescence anisotropy decay study <strong>of</strong><br />

tyrosine dynamics in motilin. Biophys J 83:2812–2825.<br />

66. Kroes SJ, Canters GW, Gilardi G, van Hoek A, Visser AJWG. 1998.<br />

Time-resolved fluorescence study <strong>of</strong> azurin variants: conformational<br />

heterogeneity and tryptophan mobility. Biophys J 75:2441–2450.<br />

67. Tcherkasskaya O, Ptitsyn OB, Knutson JR. 2000. Nanosecond<br />

dynamics <strong>of</strong> tryptophans in different conformational states <strong>of</strong><br />

apomyoglobin proteins. Biochemistry 39:1879–1889.<br />

68. Lakshmikanth GS, Krishnamoorthy G. 1999. Solvent-exposed tryptophans<br />

probe the dynamics at protein surfaces. Biophys J<br />

77:1100–1106.<br />

69. Kouyama I, Kinosita K, Ikegami A. 1989. Correlation between internal<br />

motion and emission kinetics <strong>of</strong> tryptophan residues in proteins.<br />

Eur J Biochem 182:517–521.<br />

70. Hansen JE, Rosenthal SJ, Fleming GR. 1992. Subpicosecond fluorescence<br />

depolarization studies <strong>of</strong> tryptophan and tryptophanyl<br />

residues <strong>of</strong> proteins. J Phys Chem 96:3034–3040.<br />

71. Ross JBA, Rousslang KW, Brand L. 1981. Time-resolved fluorescence<br />

and anisotropy decay <strong>of</strong> the tryptophan in adrenocorticotropin-<br />

(1-24). Biochemistry 20:4361–4369.<br />

72. Nordlund TM, Podolski DA. 1983. Streak camera measurement <strong>of</strong><br />

tryptophan and rhodamine motions with picosecond time resolution.<br />

Photochem Photobiol 38(6):665–669.<br />

73. Nordlund TM, Liu X-Y, Sommer JH. 1986. <strong>Fluorescence</strong> polarization<br />

decay <strong>of</strong> tyrosine in lima bean trypsin inhibitor. Proc Natl Acad<br />

Sci USA 83:8977–8981.<br />

74. Data courtesy <strong>of</strong> Dr. John Lee, University <strong>of</strong> Georgia.<br />

75. Liao R, Wang C-K, Cheung HC. 1992. Time-resolved tryptophan<br />

emission study <strong>of</strong> cardiac troponin I. Biophys J 63:986–995.<br />

76. Dittes K, Gakamsky DM, Haran G, Haas E, Ojcius DM, Kourilsky P,<br />

Pecht I. 1994. Picosecond fluorescence spectroscopy <strong>of</strong> a singlechain<br />

class I major histocompatibility complex encoded protein in its<br />

peptide loaded and unloaded states. Immunol Lett 40:125–132.

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