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From the same journal

FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS

Research output: Contribution to journal › Article › peer-review

Standard

FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES) : RELATION TO X-RAY MODELS. / GENOV, N ; NICOLOV, P ; BETZEL, C ; WILSON, K ; DOLASHKA, P .

In: JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, Vol. 18, No. 2-3, 05.1993, p. 265-272.

Research output: Contribution to journal › Article › peer-review

Harvard

GENOV, N, NICOLOV, P, BETZEL, C, WILSON, K & DOLASHKA, P 1993, 'FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS', JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, vol. 18, no. 2-3, pp. 265-272.

APA

GENOV, N., NICOLOV, P., BETZEL, C., WILSON, K., & DOLASHKA, P. (1993). FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS. JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 18(2-3), 265-272.

Vancouver

GENOV N, NICOLOV P, BETZEL C, WILSON K, DOLASHKA P. FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS. JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY. 1993 May;18(2-3):265-272.

Author

GENOV, N ; NICOLOV, P ; BETZEL, C ; WILSON, K ; DOLASHKA, P . / FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES) : RELATION TO X-RAY MODELS. In: JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY. 1993 ; Vol. 18, No. 2-3. pp. 265-272.

Bibtex - Download

@article{7db491377c1149f39688019781d41c30,
title = "FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES): RELATION TO X-RAY MODELS",
abstract = "The fluorescence properties of six subtilases with known X-ray structure were determined using the same experimental conditions and instrumentation. The steady state and nanosecond lifetime measurements were performed on purified samples of phenylmethanesulphonyl-inhibited proteinases in the presence of 20 mM CaCl2 which stabilizes the molecules. The tryptophan emission quantum yield strongly depends on the local environment and varies from 0.02 to 0.10. The efficiency of tyrosine-to-tryptophan energy transfer also varies (O%-70%) in the different enzymes; the most efficient transfer was observed for thermitase.Experiments with nanosecond excitation indicated that the tryptophan fluorescence of subtilases decays with two exponential components. The X-ray models of the six proteinases were analysed in the region of the tryptophyl residues and were used to explain the observed properties.",
author = "N GENOV and P NICOLOV and C BETZEL and K WILSON and P DOLASHKA",
year = "1993",
month = may,
language = "English",
volume = "18",
pages = "265--272",
journal = "JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY",
issn = "1011-1344",
publisher = "Elsevier",
number = "2-3",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - FLUORESCENCE PROPERTIES OF SUBTILISINS AND RELATED PROTEINASES (SUBTILASES)

T2 - RELATION TO X-RAY MODELS

AU - GENOV, N

AU - NICOLOV, P

AU - BETZEL, C

AU - WILSON, K

AU - DOLASHKA, P

PY - 1993/5

Y1 - 1993/5

N2 - The fluorescence properties of six subtilases with known X-ray structure were determined using the same experimental conditions and instrumentation. The steady state and nanosecond lifetime measurements were performed on purified samples of phenylmethanesulphonyl-inhibited proteinases in the presence of 20 mM CaCl2 which stabilizes the molecules. The tryptophan emission quantum yield strongly depends on the local environment and varies from 0.02 to 0.10. The efficiency of tyrosine-to-tryptophan energy transfer also varies (O%-70%) in the different enzymes; the most efficient transfer was observed for thermitase.Experiments with nanosecond excitation indicated that the tryptophan fluorescence of subtilases decays with two exponential components. The X-ray models of the six proteinases were analysed in the region of the tryptophyl residues and were used to explain the observed properties.

AB - The fluorescence properties of six subtilases with known X-ray structure were determined using the same experimental conditions and instrumentation. The steady state and nanosecond lifetime measurements were performed on purified samples of phenylmethanesulphonyl-inhibited proteinases in the presence of 20 mM CaCl2 which stabilizes the molecules. The tryptophan emission quantum yield strongly depends on the local environment and varies from 0.02 to 0.10. The efficiency of tyrosine-to-tryptophan energy transfer also varies (O%-70%) in the different enzymes; the most efficient transfer was observed for thermitase.Experiments with nanosecond excitation indicated that the tryptophan fluorescence of subtilases decays with two exponential components. The X-ray models of the six proteinases were analysed in the region of the tryptophyl residues and were used to explain the observed properties.

M3 - Article

VL - 18

SP - 265

EP - 272

JO - JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY

JF - JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY

SN - 1011-1344

IS - 2-3

ER -

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