Solid state NMR studies of molecular recognition at protein-mineral interfaces

Gil Goobes; Patrick S. Stayton; Gary P. Drobny

doi:10.1016/j.pnmrs.2006.11.002

Solid state NMR studies of molecular recognition at protein-mineral interfaces

Gil Goobes, Patrick S. Stayton, Gary P. Drobny

University of Washington

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

49 Scopus citations

Abstract

The use of nuclear magnetic resonance (NMR) to analyze the structure and crystal recognition mechanisms of an salivary protein model system is described. NMR dipolar coupling measurements are used to obtain high resolution structures for proteins in microcrystalline form, for proteins oriented in lipid bilayers and lipid vesicles and for proteins in fibrillar form. NMR pulse techniques are also capable of reporting the structures of surface-adsorbed proteins and protein-crystal interactions in molecular detail. The investigations of protein mineral interactions are frequently conducted with techniques that characterize the macroscopic behavior of proteins in the presence of mineral crystals. Equilibrium properties are derived via adsorption isotherm measurements, where data are usually analyzed by assuming a simple Langmuir model of protein adsorption onto the crystal faces.

Original language	English
Pages (from-to)	71-85
Number of pages	15
Journal	Progress in Nuclear Magnetic Resonance Spectroscopy
Volume	50
Issue number	2-3
DOIs	https://doi.org/10.1016/j.pnmrs.2006.11.002
State	Published - 30 May 2007
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by the NSF (Grants EEC 9529161 and DMR 0110505) and the National Dental Institute (Grant DE-12554). In addition, many people contributed to the statherin NMR/structural modelling project. NMR studies of the structure of the N-terminus of statherin as well as studies of the structures of peptides derived from the N-terminus were conducted by J.R. Long and W.J. Shaw. NMR studies of statherin side chain interactions with HAP were conducted by V. Raghunathan, J.M. Gibson, and J.M. Popham. Samples of multiply labelled statherin were provided by R. Goobes. NMR experiments on multiply labelled statherin samples were performed by G. Goobes. The ROSETTA program was developed in the laboratory of D. Baker. O. Schueler-Furman produced ROSETTA-based models of statherin. We thank Nicholas Breen for proof-reading the manuscript and for helpful discussions.

Funding

This work was supported by the NSF (Grants EEC 9529161 and DMR 0110505) and the National Dental Institute (Grant DE-12554). In addition, many people contributed to the statherin NMR/structural modelling project. NMR studies of the structure of the N-terminus of statherin as well as studies of the structures of peptides derived from the N-terminus were conducted by J.R. Long and W.J. Shaw. NMR studies of statherin side chain interactions with HAP were conducted by V. Raghunathan, J.M. Gibson, and J.M. Popham. Samples of multiply labelled statherin were provided by R. Goobes. NMR experiments on multiply labelled statherin samples were performed by G. Goobes. The ROSETTA program was developed in the laboratory of D. Baker. O. Schueler-Furman produced ROSETTA-based models of statherin. We thank Nicholas Breen for proof-reading the manuscript and for helpful discussions.

Funders	Funder number
National Dental Institute	DE-12554
National Science Foundation	EEC 9529161, DMR 0110505

Keywords

Adsorbed protein
Biomineralization
Magic angle spinning
Recoupling
Structure determination

Access to Document

10.1016/j.pnmrs.2006.11.002

Cite this

@article{20aa1612915a464ab1cf0d1215e9c60f,

title = "Solid state NMR studies of molecular recognition at protein-mineral interfaces",

abstract = "The use of nuclear magnetic resonance (NMR) to analyze the structure and crystal recognition mechanisms of an salivary protein model system is described. NMR dipolar coupling measurements are used to obtain high resolution structures for proteins in microcrystalline form, for proteins oriented in lipid bilayers and lipid vesicles and for proteins in fibrillar form. NMR pulse techniques are also capable of reporting the structures of surface-adsorbed proteins and protein-crystal interactions in molecular detail. The investigations of protein mineral interactions are frequently conducted with techniques that characterize the macroscopic behavior of proteins in the presence of mineral crystals. Equilibrium properties are derived via adsorption isotherm measurements, where data are usually analyzed by assuming a simple Langmuir model of protein adsorption onto the crystal faces.",

keywords = "Adsorbed protein, Biomineralization, Magic angle spinning, Recoupling, Structure determination",

author = "Gil Goobes and Stayton, {Patrick S.} and Drobny, {Gary P.}",

note = "Funding Information: This work was supported by the NSF (Grants EEC 9529161 and DMR 0110505) and the National Dental Institute (Grant DE-12554). In addition, many people contributed to the statherin NMR/structural modelling project. NMR studies of the structure of the N-terminus of statherin as well as studies of the structures of peptides derived from the N-terminus were conducted by J.R. Long and W.J. Shaw. NMR studies of statherin side chain interactions with HAP were conducted by V. Raghunathan, J.M. Gibson, and J.M. Popham. Samples of multiply labelled statherin were provided by R. Goobes. NMR experiments on multiply labelled statherin samples were performed by G. Goobes. The ROSETTA program was developed in the laboratory of D. Baker. O. Schueler-Furman produced ROSETTA-based models of statherin. We thank Nicholas Breen for proof-reading the manuscript and for helpful discussions. ",

year = "2007",

month = may,

day = "30",

doi = "10.1016/j.pnmrs.2006.11.002",

language = "אנגלית",

volume = "50",

pages = "71--85",

journal = "Progress in Nuclear Magnetic Resonance Spectroscopy",

issn = "0079-6565",

publisher = "Elsevier B.V.",

number = "2-3",

}

TY - JOUR

T1 - Solid state NMR studies of molecular recognition at protein-mineral interfaces

AU - Goobes, Gil

AU - Stayton, Patrick S.

AU - Drobny, Gary P.

N1 - Funding Information: This work was supported by the NSF (Grants EEC 9529161 and DMR 0110505) and the National Dental Institute (Grant DE-12554). In addition, many people contributed to the statherin NMR/structural modelling project. NMR studies of the structure of the N-terminus of statherin as well as studies of the structures of peptides derived from the N-terminus were conducted by J.R. Long and W.J. Shaw. NMR studies of statherin side chain interactions with HAP were conducted by V. Raghunathan, J.M. Gibson, and J.M. Popham. Samples of multiply labelled statherin were provided by R. Goobes. NMR experiments on multiply labelled statherin samples were performed by G. Goobes. The ROSETTA program was developed in the laboratory of D. Baker. O. Schueler-Furman produced ROSETTA-based models of statherin. We thank Nicholas Breen for proof-reading the manuscript and for helpful discussions.

PY - 2007/5/30

Y1 - 2007/5/30

N2 - The use of nuclear magnetic resonance (NMR) to analyze the structure and crystal recognition mechanisms of an salivary protein model system is described. NMR dipolar coupling measurements are used to obtain high resolution structures for proteins in microcrystalline form, for proteins oriented in lipid bilayers and lipid vesicles and for proteins in fibrillar form. NMR pulse techniques are also capable of reporting the structures of surface-adsorbed proteins and protein-crystal interactions in molecular detail. The investigations of protein mineral interactions are frequently conducted with techniques that characterize the macroscopic behavior of proteins in the presence of mineral crystals. Equilibrium properties are derived via adsorption isotherm measurements, where data are usually analyzed by assuming a simple Langmuir model of protein adsorption onto the crystal faces.

AB - The use of nuclear magnetic resonance (NMR) to analyze the structure and crystal recognition mechanisms of an salivary protein model system is described. NMR dipolar coupling measurements are used to obtain high resolution structures for proteins in microcrystalline form, for proteins oriented in lipid bilayers and lipid vesicles and for proteins in fibrillar form. NMR pulse techniques are also capable of reporting the structures of surface-adsorbed proteins and protein-crystal interactions in molecular detail. The investigations of protein mineral interactions are frequently conducted with techniques that characterize the macroscopic behavior of proteins in the presence of mineral crystals. Equilibrium properties are derived via adsorption isotherm measurements, where data are usually analyzed by assuming a simple Langmuir model of protein adsorption onto the crystal faces.

KW - Adsorbed protein

KW - Biomineralization

KW - Magic angle spinning

KW - Recoupling

KW - Structure determination

UR - http://www.scopus.com/inward/record.url?scp=33847636366&partnerID=8YFLogxK

U2 - 10.1016/j.pnmrs.2006.11.002

DO - 10.1016/j.pnmrs.2006.11.002

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.systematicreview???

AN - SCOPUS:33847636366

SN - 0079-6565

VL - 50

SP - 71

EP - 85

JO - Progress in Nuclear Magnetic Resonance Spectroscopy

JF - Progress in Nuclear Magnetic Resonance Spectroscopy

IS - 2-3

ER -

Solid state NMR studies of molecular recognition at protein-mineral interfaces

Abstract

Bibliographical note

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this