Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

Paul R. Carey; Munsok Kim; Peter J. Tonge

doi:10.1117/12.57334

Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

Paul R. Carey
, Munsok Kim
, Peter J. Tonge

Chemistry

National Research Council of Canada

Research output: Contribution to journal › Conference article › peer-review

Abstract

Resonance Raman spectra for enzyme-substrate intermediates of the type R(C=C)NHCH₂C(=S)S-Papain are reported in solution at 300 K and down to 4 K in ice matrices. Analysis reveals that the overall conformation of the substrate-enzyme bonds in the active site remains the same in the range 300 - 4 K but there are important minor spectral changes. Some of these provide access to information on dynamical fluctuations occurring in the active site. Evidence for closely lying fluctuating protein states driving fluctuations in the structure of the bound substrate is discussed.

Original language	English
Pages (from-to)	37-39
Number of pages	3
Journal	Proceedings of SPIE - The International Society for Optical Engineering
Volume	1403
Issue number	pt 1
DOIs	https://doi.org/10.1117/12.57334
State	Published - 1991
Event	International Conference on Laser Applications in Life Sciences - Moscow, USSR Duration: Aug 27 1990 → Aug 31 1990

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title = "Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy",

abstract = "Resonance Raman spectra for enzyme-substrate intermediates of the type R(C=C)NHCH2C(=S)S-Papain are reported in solution at 300 K and down to 4 K in ice matrices. Analysis reveals that the overall conformation of the substrate-enzyme bonds in the active site remains the same in the range 300 - 4 K but there are important minor spectral changes. Some of these provide access to information on dynamical fluctuations occurring in the active site. Evidence for closely lying fluctuating protein states driving fluctuations in the structure of the bound substrate is discussed.",

author = "Carey, \{Paul R.\} and Munsok Kim and Tonge, \{Peter J.\}",

year = "1991",

doi = "10.1117/12.57334",

language = "English",

volume = "1403",

pages = "37--39",

journal = "Proceedings of SPIE - The International Society for Optical Engineering",

issn = "0277-786X",

number = "pt 1",

note = "International Conference on Laser Applications in Life Sciences ; Conference date: 27-08-1990 Through 31-08-1990",

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TY - JOUR

T1 - Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

AU - Carey, Paul R.

AU - Kim, Munsok

AU - Tonge, Peter J.

PY - 1991

Y1 - 1991

N2 - Resonance Raman spectra for enzyme-substrate intermediates of the type R(C=C)NHCH2C(=S)S-Papain are reported in solution at 300 K and down to 4 K in ice matrices. Analysis reveals that the overall conformation of the substrate-enzyme bonds in the active site remains the same in the range 300 - 4 K but there are important minor spectral changes. Some of these provide access to information on dynamical fluctuations occurring in the active site. Evidence for closely lying fluctuating protein states driving fluctuations in the structure of the bound substrate is discussed.

AB - Resonance Raman spectra for enzyme-substrate intermediates of the type R(C=C)NHCH2C(=S)S-Papain are reported in solution at 300 K and down to 4 K in ice matrices. Analysis reveals that the overall conformation of the substrate-enzyme bonds in the active site remains the same in the range 300 - 4 K but there are important minor spectral changes. Some of these provide access to information on dynamical fluctuations occurring in the active site. Evidence for closely lying fluctuating protein states driving fluctuations in the structure of the bound substrate is discussed.

UR - https://www.scopus.com/pages/publications/0025742002

U2 - 10.1117/12.57334

DO - 10.1117/12.57334

M3 - Conference article

AN - SCOPUS:0025742002

SN - 0277-786X

VL - 1403

SP - 37

EP - 39

JO - Proceedings of SPIE - The International Society for Optical Engineering

JF - Proceedings of SPIE - The International Society for Optical Engineering

IS - pt 1

T2 - International Conference on Laser Applications in Life Sciences

Y2 - 27 August 1990 through 31 August 1990

ER -

Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

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