Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs)

Louise Butt; Robert Holland; Nikul Satish Khunti; Debra Quinn; Andrew Pickford

doi:10.1007/978-1-4939-6863-3_6

Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs)

Louise Butt, Robert Holland, Nikul Satish Khunti, Debra Quinn, Andrew Pickford

Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed) › peer-review

Abstract

Small angle X-ray scattering (SAXS) provides information about the conformation and flexibility of proteins in solution, and hence provides complementary structural information to that obtained from X-ray crystallography and nuclear magnetic resonance spectroscopy. In this chapter, we describe the methods for the preparation of matrix metalloproteinase (MMP) samples for SAXS analyses, and for the acquisition, processing and interpretation of the SAXS data.

Original language	English
Title of host publication	Matrix metalloproteases
Subtitle of host publication	methods and protocols
Editors	Charles Galea
Publisher	Humana Press
Pages	87-108
Number of pages	22
Volume	1579
Edition	1
ISBN (Electronic)	978-1493968633
ISBN (Print)	978-1493968619
DOIs	https://doi.org/10.1007/978-1-4939-6863-3_6
Publication status	Published - 16 Mar 2017

Publication series

Name	Methods in Molecular Biology
Volume	1579
ISSN (Print)	1064-3745

Keywords

protein dynamics
protein flexibility
multi-domain
oligomer
structure-function relationship

Access to Document

10.1007/978-1-4939-6863-3_6

https://www.palgrave.com/de/book/9781493968619

Cite this

Butt, L., Holland, R., Khunti, N. S., Quinn, D., & Pickford, A. (2017). Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs). In C. Galea (Ed.), Matrix metalloproteases: methods and protocols (1 ed., Vol. 1579, pp. 87-108). (Methods in Molecular Biology; Vol. 1579). Humana Press. https://doi.org/10.1007/978-1-4939-6863-3_6

@inbook{d3908c1995ad4b77acbfa2982eaba196,

title = "Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs)",

abstract = "Small angle X-ray scattering (SAXS) provides information about the conformation and flexibility of proteins in solution, and hence provides complementary structural information to that obtained from X-ray crystallography and nuclear magnetic resonance spectroscopy. In this chapter, we describe the methods for the preparation of matrix metalloproteinase (MMP) samples for SAXS analyses, and for the acquisition, processing and interpretation of the SAXS data.",

keywords = "protein dynamics, protein flexibility, multi-domain, oligomer, structure-function relationship",

author = "Louise Butt and Robert Holland and Khunti, {Nikul Satish} and Debra Quinn and Andrew Pickford",

year = "2017",

month = mar,

day = "16",

doi = "10.1007/978-1-4939-6863-3_6",

language = "English",

isbn = "978-1493968619",

volume = "1579",

series = "Methods in Molecular Biology",

publisher = "Humana Press",

pages = "87--108",

editor = "Charles Galea",

booktitle = "Matrix metalloproteases",

address = "United States",

edition = "1",

}

Butt, L, Holland, R, Khunti, NS, Quinn, D & Pickford, A 2017, Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs). in C Galea (ed.), Matrix metalloproteases: methods and protocols. 1 edn, vol. 1579, Methods in Molecular Biology, vol. 1579, Humana Press, pp. 87-108. https://doi.org/10.1007/978-1-4939-6863-3_6

Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs). / Butt, Louise; Holland, Robert; Khunti, Nikul Satish et al.
Matrix metalloproteases: methods and protocols. ed. / Charles Galea. Vol. 1579 1. ed. Humana Press, 2017. p. 87-108 (Methods in Molecular Biology; Vol. 1579).

Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed) › peer-review

TY - CHAP

T1 - Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs)

AU - Butt, Louise

AU - Holland, Robert

AU - Khunti, Nikul Satish

AU - Quinn, Debra

AU - Pickford, Andrew

PY - 2017/3/16

Y1 - 2017/3/16

N2 - Small angle X-ray scattering (SAXS) provides information about the conformation and flexibility of proteins in solution, and hence provides complementary structural information to that obtained from X-ray crystallography and nuclear magnetic resonance spectroscopy. In this chapter, we describe the methods for the preparation of matrix metalloproteinase (MMP) samples for SAXS analyses, and for the acquisition, processing and interpretation of the SAXS data.

AB - Small angle X-ray scattering (SAXS) provides information about the conformation and flexibility of proteins in solution, and hence provides complementary structural information to that obtained from X-ray crystallography and nuclear magnetic resonance spectroscopy. In this chapter, we describe the methods for the preparation of matrix metalloproteinase (MMP) samples for SAXS analyses, and for the acquisition, processing and interpretation of the SAXS data.

KW - protein dynamics

KW - protein flexibility

KW - multi-domain

KW - oligomer

KW - structure-function relationship

U2 - 10.1007/978-1-4939-6863-3_6

DO - 10.1007/978-1-4939-6863-3_6

M3 - Chapter (peer-reviewed)

SN - 978-1493968619

VL - 1579

T3 - Methods in Molecular Biology

SP - 87

EP - 108

BT - Matrix metalloproteases

A2 - Galea, Charles

PB - Humana Press

ER -

Using Small angle X-ray acattering (SAXS) to characterise the solution conformation and flexibility of matrix metalloproteinases (MMPs)

Abstract

Publication series

Keywords

Access to Document

Fingerprint

Cite this