Vliianie modifikatsii ostatka lizina-83 na termostabil'nost' subfragmenta 1 miozina i ee izmeneniia, vyzvaemye sviazyvaniem nukleotidov

D. A. Pavlov; A. A. Bobkov; O. P. Nikolaeva; N. N. Magretova; I. V. Dedova; D. I. Levitskiǐ

Vliianie modifikatsii ostatka lizina-83 na termostabil'nost' subfragmenta 1 miozina i ee izmeneniia, vyzvaemye sviazyvaniem nukleotidov

Translated title of the contribution: The effect of modifying the lysine-83 residue on the thermal stability of myosin subfragment 1 and changes in it caused by nucleotide binding

D. A. Pavlov^*, A. A. Bobkov, O. P. Nikolaeva, N. N. Magretova, I. V. Dedova, D. I. Levitskiǐ

^*Corresponding author for this work

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

1 Citation (Scopus)

Abstract

The effects of trinitrophenylation of lysyl residues of rabbit skeletal myosin subfragment 1 (S1) on thermal denaturation of S1 in the absence of nucleotides, in the presence of ADP and within S1 complexes with ADP and Pi analogues, orthovanadate (Vi) or beryllium fluoride (BeFx), have been studied by differential scanning calorimetry. It has been shown that lysyl trinitrophenylation significantly affects the thermal stability of S1, changes its domain structure, promotes the decomposition of S1.ADP.Vi and S1.ADP.BeFx complexes, and strongly prevents the structural changes in the S1 molecule induced by the formation of the S1.ADP.Vi complex without any effect on the thermal stability of S1 within S1.ADP and S1.ADP.BeFx complexes. It has been demonstrated that the effects of trinitrophenylation on the S1 structure are mainly due to specific modification of the epsilon-amino group of the Lys-83 residue.

Translated title of the contribution	The effect of modifying the lysine-83 residue on the thermal stability of myosin subfragment 1 and changes in it caused by nucleotide binding
Original language	Russian
Pages (from-to)	1100-1110
Number of pages	11
Journal	Biokhimiya
Volume	60
Issue number	7
Publication status	Published - Jul 1995
Externally published	Yes

Cite this

@article{eb0e4fab93824f318fd8cecdd561ce81,

title = "Vliianie modifikatsii ostatka lizina-83 na termostabil'nost' subfragmenta 1 miozina i ee izmeneniia, vyzvaemye sviazyvaniem nukleotidov",

abstract = "The effects of trinitrophenylation of lysyl residues of rabbit skeletal myosin subfragment 1 (S1) on thermal denaturation of S1 in the absence of nucleotides, in the presence of ADP and within S1 complexes with ADP and Pi analogues, orthovanadate (Vi) or beryllium fluoride (BeFx), have been studied by differential scanning calorimetry. It has been shown that lysyl trinitrophenylation significantly affects the thermal stability of S1, changes its domain structure, promotes the decomposition of S1.ADP.Vi and S1.ADP.BeFx complexes, and strongly prevents the structural changes in the S1 molecule induced by the formation of the S1.ADP.Vi complex without any effect on the thermal stability of S1 within S1.ADP and S1.ADP.BeFx complexes. It has been demonstrated that the effects of trinitrophenylation on the S1 structure are mainly due to specific modification of the epsilon-amino group of the Lys-83 residue.",

author = "Pavlov, {D. A.} and Bobkov, {A. A.} and Nikolaeva, {O. P.} and Magretova, {N. N.} and Dedova, {I. V.} and Levitskiǐ, {D. I.}",

year = "1995",

month = jul,

language = "Russian",

volume = "60",

pages = "1100--1110",

journal = "Biokhimiya",

issn = "0320-9725",

publisher = "Izdatel'stvo Nauka",

number = "7",

}

TY - JOUR

T1 - Vliianie modifikatsii ostatka lizina-83 na termostabil'nost' subfragmenta 1 miozina i ee izmeneniia, vyzvaemye sviazyvaniem nukleotidov

AU - Pavlov, D. A.

AU - Bobkov, A. A.

AU - Nikolaeva, O. P.

AU - Magretova, N. N.

AU - Dedova, I. V.

AU - Levitskiǐ, D. I.

PY - 1995/7

Y1 - 1995/7

N2 - The effects of trinitrophenylation of lysyl residues of rabbit skeletal myosin subfragment 1 (S1) on thermal denaturation of S1 in the absence of nucleotides, in the presence of ADP and within S1 complexes with ADP and Pi analogues, orthovanadate (Vi) or beryllium fluoride (BeFx), have been studied by differential scanning calorimetry. It has been shown that lysyl trinitrophenylation significantly affects the thermal stability of S1, changes its domain structure, promotes the decomposition of S1.ADP.Vi and S1.ADP.BeFx complexes, and strongly prevents the structural changes in the S1 molecule induced by the formation of the S1.ADP.Vi complex without any effect on the thermal stability of S1 within S1.ADP and S1.ADP.BeFx complexes. It has been demonstrated that the effects of trinitrophenylation on the S1 structure are mainly due to specific modification of the epsilon-amino group of the Lys-83 residue.

AB - The effects of trinitrophenylation of lysyl residues of rabbit skeletal myosin subfragment 1 (S1) on thermal denaturation of S1 in the absence of nucleotides, in the presence of ADP and within S1 complexes with ADP and Pi analogues, orthovanadate (Vi) or beryllium fluoride (BeFx), have been studied by differential scanning calorimetry. It has been shown that lysyl trinitrophenylation significantly affects the thermal stability of S1, changes its domain structure, promotes the decomposition of S1.ADP.Vi and S1.ADP.BeFx complexes, and strongly prevents the structural changes in the S1 molecule induced by the formation of the S1.ADP.Vi complex without any effect on the thermal stability of S1 within S1.ADP and S1.ADP.BeFx complexes. It has been demonstrated that the effects of trinitrophenylation on the S1 structure are mainly due to specific modification of the epsilon-amino group of the Lys-83 residue.

UR - http://www.scopus.com/inward/record.url?scp=0029337804&partnerID=8YFLogxK

M3 - Article

C2 - 7578566

AN - SCOPUS:0029337804

SN - 0320-9725

VL - 60

SP - 1100

EP - 1110

JO - Biokhimiya

JF - Biokhimiya

IS - 7

ER -

Vliianie modifikatsii ostatka lizina-83 na termostabil'nost' subfragmenta 1 miozina i ee izmeneniia, vyzvaemye sviazyvaniem nukleotidov

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