Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor β-sheet NH's

I. Simon, Erik Tüchsen, Clare Woodward

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The hydrogen-deuterium exchange rates of the slowest exchanging β-sheet NH's in the bovine pancreatic trypsin inhibitor (BPTI) have been determined in free BPTI and in the trypsin-BPTI complex at pH 9-10, 25-40 °C. Rate constants for individual protons have been measured from their assigned resonances in the 1H NMR spectrum. Trypsin binding has a highly localized effect; the Tyr-35 NH exchange rate is slowed by a factor of >103 in the complex, while the other NH's measured are slowed by a factor of 3-15. In free BPTI, under conditions where the exchange rate constants have activation energies in the range 11-32 kcal/mol, the NH's of Tyr-21, Phe-22, and Tyr-23 are several orders of magnitude slower than the other β-sheet NH's.

Original languageEnglish
Pages (from-to)2064-2068
Number of pages5
JournalBiochemistry
Volume23
Issue number9
Publication statusPublished - 1984

Fingerprint

Aprotinin
Trypsin
Hydrogen
Kinetics
Rate constants
Deuterium
Protons
Activation energy
Nuclear magnetic resonance

ASJC Scopus subject areas

  • Biochemistry

Cite this

Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor β-sheet NH's. / Simon, I.; Tüchsen, Erik; Woodward, Clare.

In: Biochemistry, Vol. 23, No. 9, 1984, p. 2064-2068.

Research output: Contribution to journalArticle

@article{8a1148247326413195060046657c04c6,
title = "Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor β-sheet NH's",
abstract = "The hydrogen-deuterium exchange rates of the slowest exchanging β-sheet NH's in the bovine pancreatic trypsin inhibitor (BPTI) have been determined in free BPTI and in the trypsin-BPTI complex at pH 9-10, 25-40 °C. Rate constants for individual protons have been measured from their assigned resonances in the 1H NMR spectrum. Trypsin binding has a highly localized effect; the Tyr-35 NH exchange rate is slowed by a factor of >103 in the complex, while the other NH's measured are slowed by a factor of 3-15. In free BPTI, under conditions where the exchange rate constants have activation energies in the range 11-32 kcal/mol, the NH's of Tyr-21, Phe-22, and Tyr-23 are several orders of magnitude slower than the other β-sheet NH's.",
author = "I. Simon and Erik T{\"u}chsen and Clare Woodward",
year = "1984",
language = "English",
volume = "23",
pages = "2064--2068",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "9",

}

TY - JOUR

T1 - Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor β-sheet NH's

AU - Simon, I.

AU - Tüchsen, Erik

AU - Woodward, Clare

PY - 1984

Y1 - 1984

N2 - The hydrogen-deuterium exchange rates of the slowest exchanging β-sheet NH's in the bovine pancreatic trypsin inhibitor (BPTI) have been determined in free BPTI and in the trypsin-BPTI complex at pH 9-10, 25-40 °C. Rate constants for individual protons have been measured from their assigned resonances in the 1H NMR spectrum. Trypsin binding has a highly localized effect; the Tyr-35 NH exchange rate is slowed by a factor of >103 in the complex, while the other NH's measured are slowed by a factor of 3-15. In free BPTI, under conditions where the exchange rate constants have activation energies in the range 11-32 kcal/mol, the NH's of Tyr-21, Phe-22, and Tyr-23 are several orders of magnitude slower than the other β-sheet NH's.

AB - The hydrogen-deuterium exchange rates of the slowest exchanging β-sheet NH's in the bovine pancreatic trypsin inhibitor (BPTI) have been determined in free BPTI and in the trypsin-BPTI complex at pH 9-10, 25-40 °C. Rate constants for individual protons have been measured from their assigned resonances in the 1H NMR spectrum. Trypsin binding has a highly localized effect; the Tyr-35 NH exchange rate is slowed by a factor of >103 in the complex, while the other NH's measured are slowed by a factor of 3-15. In free BPTI, under conditions where the exchange rate constants have activation energies in the range 11-32 kcal/mol, the NH's of Tyr-21, Phe-22, and Tyr-23 are several orders of magnitude slower than the other β-sheet NH's.

UR - http://www.scopus.com/inward/record.url?scp=0038964082&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038964082&partnerID=8YFLogxK

M3 - Article

VL - 23

SP - 2064

EP - 2068

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 9

ER -