ATP sensitive tryptophans of hsp90

Bence B. Bartha, Katalin Ajtai, David O. Toft, Thomas P Burghardt

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature. ATP and acrylamide quench the fluorescence from tryptophan free in solution principally by static and collisional mechanisms, respectively. Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible. ATP quenching of tryptopban fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism, However, ATP competitively inhibits acrylamide quenching of the readily accessible class of tryptophan residues by static quenching with the quenching constant providing an upper limit for the ATP dissociation constant. The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific. The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.

Original languageEnglish (US)
Pages (from-to)313-321
Number of pages9
JournalBiophysical Chemistry
Volume72
Issue number3
DOIs
StatePublished - Jun 9 1998

Fingerprint

adenosine triphosphate
tryptophan
Tryptophan
Adenosine Triphosphate
Quenching
quenching
Fluorescence
Acrylamide
fluorescence
nucleotides
Nucleotides
dissociation
proximity
interactions
Temperature

Keywords

  • Acrylamide
  • Conformation
  • Fluorescence quenching
  • Nucleotide binding

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Biophysics

Cite this

Bartha, B. B., Ajtai, K., Toft, D. O., & Burghardt, T. P. (1998). ATP sensitive tryptophans of hsp90. Biophysical Chemistry, 72(3), 313-321. https://doi.org/10.1016/S0301-4622(98)00114-8

ATP sensitive tryptophans of hsp90. / Bartha, Bence B.; Ajtai, Katalin; Toft, David O.; Burghardt, Thomas P.

In: Biophysical Chemistry, Vol. 72, No. 3, 09.06.1998, p. 313-321.

Research output: Contribution to journalArticle

Bartha, BB, Ajtai, K, Toft, DO & Burghardt, TP 1998, 'ATP sensitive tryptophans of hsp90', Biophysical Chemistry, vol. 72, no. 3, pp. 313-321. https://doi.org/10.1016/S0301-4622(98)00114-8
Bartha BB, Ajtai K, Toft DO, Burghardt TP. ATP sensitive tryptophans of hsp90. Biophysical Chemistry. 1998 Jun 9;72(3):313-321. https://doi.org/10.1016/S0301-4622(98)00114-8
Bartha, Bence B. ; Ajtai, Katalin ; Toft, David O. ; Burghardt, Thomas P. / ATP sensitive tryptophans of hsp90. In: Biophysical Chemistry. 1998 ; Vol. 72, No. 3. pp. 313-321.
@article{53e18af98c0349c9be8b3e074cfe263a,
title = "ATP sensitive tryptophans of hsp90",
abstract = "The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature. ATP and acrylamide quench the fluorescence from tryptophan free in solution principally by static and collisional mechanisms, respectively. Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible. ATP quenching of tryptopban fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism, However, ATP competitively inhibits acrylamide quenching of the readily accessible class of tryptophan residues by static quenching with the quenching constant providing an upper limit for the ATP dissociation constant. The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific. The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.",
keywords = "Acrylamide, Conformation, Fluorescence quenching, Nucleotide binding",
author = "Bartha, {Bence B.} and Katalin Ajtai and Toft, {David O.} and Burghardt, {Thomas P}",
year = "1998",
month = "6",
day = "9",
doi = "10.1016/S0301-4622(98)00114-8",
language = "English (US)",
volume = "72",
pages = "313--321",
journal = "Biophysical Chemistry",
issn = "0301-4622",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - ATP sensitive tryptophans of hsp90

AU - Bartha, Bence B.

AU - Ajtai, Katalin

AU - Toft, David O.

AU - Burghardt, Thomas P

PY - 1998/6/9

Y1 - 1998/6/9

N2 - The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature. ATP and acrylamide quench the fluorescence from tryptophan free in solution principally by static and collisional mechanisms, respectively. Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible. ATP quenching of tryptopban fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism, However, ATP competitively inhibits acrylamide quenching of the readily accessible class of tryptophan residues by static quenching with the quenching constant providing an upper limit for the ATP dissociation constant. The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific. The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.

AB - The nature of the interaction between the nucleotide ATP and hsp90 was investigated by observing fluorescence quenching of the four tryptophan residues in hsp90 as a function of quencher type and temperature. ATP and acrylamide quench the fluorescence from tryptophan free in solution principally by static and collisional mechanisms, respectively. Acrylamide quenching of tryptophan fluorescence in hsp90 is also principally collisional and identifies two classes of residues, one readily accessible to quenching the other less accessible. ATP quenching of tryptopban fluorescence in hsp90 is more complex exhibiting no overall preferred mechanism, However, ATP competitively inhibits acrylamide quenching of the readily accessible class of tryptophan residues by static quenching with the quenching constant providing an upper limit for the ATP dissociation constant. The ATP-free tryptophan dissociation constant is more than a factor of three larger than that for ATP-hsp90 suggesting that the ATP-hsp90 interaction is specific. The static quenching of tryptophan fluorescence in hsp90 by ATP implies that the nucleotide binds in close proximity to one or more of the tryptophan residues.

KW - Acrylamide

KW - Conformation

KW - Fluorescence quenching

KW - Nucleotide binding

UR - http://www.scopus.com/inward/record.url?scp=0032499723&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032499723&partnerID=8YFLogxK

U2 - 10.1016/S0301-4622(98)00114-8

DO - 10.1016/S0301-4622(98)00114-8

M3 - Article

C2 - 9691273

AN - SCOPUS:0032499723

VL - 72

SP - 313

EP - 321

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 3

ER -