Tertiary structure variability within the quaternary states of hemoglobin: a spin label study

Michael E. Johnson; Diane M. Scholler; Brian M. Hoffman; Chien Ho

doi:10.1016/0005-2795(78)90085-5

Tertiary structure variability within the quaternary states of hemoglobin: a spin label study

Michael E. Johnson^*, Diane M. Scholler, Brian M. Hoffman, Chien Ho

^*Corresponding author for this work

Chemistry

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

2 Scopus citations

Abstract

Using variable temperature techniques, the spin label spectral resolution of hemoglobin labeled at the β93 cysteines with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide has been greatly enhanced. The effects of different ligands, inositol hexaphosphate, pH and salt concentration upon spin labeled ferrous and ferric hemoglobin indicate that the β chain tertiary structure exhibits considerable variability within the oxy and deoxy quaternary structures. From these studies ligand and spin state changes both appear to be of significance in producing structural changes; binding of inositol hexaphosphate then produces further structural changes secondary in amplitude.

Original language	English (US)
Pages (from-to)	193-205
Number of pages	13
Journal	BBA - Protein Structure
Volume	535
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(78)90085-5
State	Published - Aug 21 1978

Funding

This work was supported in part by research grants from the Illinois Research Board, the National Institutes of Health (HL-10383 and HL-13531) and the National Science Foundation (PCM 76-21469 and BM 500478). We wish to thank Dr. Harden M. McConnell for helpful suggestions during the initial phase of this project and Dr. Leslie Fung for a critical reading of the manuscript.

ASJC Scopus subject areas

General Medicine

Access to Document

10.1016/0005-2795(78)90085-5

Cite this

@article{cddb8672e0634d3b8267e7590f092b37,

title = "Tertiary structure variability within the quaternary states of hemoglobin: a spin label study",

abstract = "Using variable temperature techniques, the spin label spectral resolution of hemoglobin labeled at the β93 cysteines with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide has been greatly enhanced. The effects of different ligands, inositol hexaphosphate, pH and salt concentration upon spin labeled ferrous and ferric hemoglobin indicate that the β chain tertiary structure exhibits considerable variability within the oxy and deoxy quaternary structures. From these studies ligand and spin state changes both appear to be of significance in producing structural changes; binding of inositol hexaphosphate then produces further structural changes secondary in amplitude.",

author = "Johnson, {Michael E.} and Scholler, {Diane M.} and Hoffman, {Brian M.} and Chien Ho",

note = "Funding Information: This work was supported in part by research grants from the Illinois Research Board, the National Institutes of Health (HL-10383 and HL-13531) and the National Science Foundation (PCM 76-21469 and BM 500478). We wish to thank Dr. Harden M. McConnell for helpful suggestions during the initial phase of this project and Dr. Leslie Fung for a critical reading of the manuscript.",

year = "1978",

month = aug,

day = "21",

doi = "10.1016/0005-2795(78)90085-5",

language = "English (US)",

volume = "535",

pages = "193--205",

journal = "BBA - Protein Structure",

issn = "0005-2795",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - Tertiary structure variability within the quaternary states of hemoglobin

T2 - a spin label study

AU - Johnson, Michael E.

AU - Scholler, Diane M.

AU - Hoffman, Brian M.

AU - Ho, Chien

N1 - Funding Information: This work was supported in part by research grants from the Illinois Research Board, the National Institutes of Health (HL-10383 and HL-13531) and the National Science Foundation (PCM 76-21469 and BM 500478). We wish to thank Dr. Harden M. McConnell for helpful suggestions during the initial phase of this project and Dr. Leslie Fung for a critical reading of the manuscript.

PY - 1978/8/21

Y1 - 1978/8/21

N2 - Using variable temperature techniques, the spin label spectral resolution of hemoglobin labeled at the β93 cysteines with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide has been greatly enhanced. The effects of different ligands, inositol hexaphosphate, pH and salt concentration upon spin labeled ferrous and ferric hemoglobin indicate that the β chain tertiary structure exhibits considerable variability within the oxy and deoxy quaternary structures. From these studies ligand and spin state changes both appear to be of significance in producing structural changes; binding of inositol hexaphosphate then produces further structural changes secondary in amplitude.

AB - Using variable temperature techniques, the spin label spectral resolution of hemoglobin labeled at the β93 cysteines with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide has been greatly enhanced. The effects of different ligands, inositol hexaphosphate, pH and salt concentration upon spin labeled ferrous and ferric hemoglobin indicate that the β chain tertiary structure exhibits considerable variability within the oxy and deoxy quaternary structures. From these studies ligand and spin state changes both appear to be of significance in producing structural changes; binding of inositol hexaphosphate then produces further structural changes secondary in amplitude.

UR - http://www.scopus.com/inward/record.url?scp=0018103011&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018103011&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(78)90085-5

DO - 10.1016/0005-2795(78)90085-5

M3 - Article

C2 - 678549

AN - SCOPUS:0018103011

SN - 0005-2795

VL - 535

SP - 193

EP - 205

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 2

ER -

Tertiary structure variability within the quaternary states of hemoglobin: a spin label study

Abstract

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this