Hyaluronan: Polysaccharide chaos to protein organisation

Anthony J. Day; John K. Sheehan

doi:10.1016/S0959-440X(00)00256-6

Hyaluronan: Polysaccharide chaos to protein organisation

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

Abstract

Molecular dynamics simulations of hyaluronan have revealed the inherent flexibility of this glycosaminoglycan in solution. Crystal structures of hyaluronan-digesting enzymes have provided the first direct insights into the molecular basis of hyaluronan-protein interactions. Various studies on hyaluronan-binding proteins suggest there is considerable diversity in their mode of interaction with hyaluronan, which might result in many different bound conformations of the polysaccharide.

Original language	English
Pages (from-to)	617-622
Number of pages	5
Journal	Current Opinion in Structural Biology
Volume	11
Issue number	5
DOIs	https://doi.org/10.1016/S0959-440X(00)00256-6
Publication status	Published - 1 Sept 2001

Access to Document

10.1016/S0959-440X(00)00256-6

Cite this

@article{2c85bed2822c4f749254cd629e6d3e3b,

title = "Hyaluronan: Polysaccharide chaos to protein organisation",

abstract = "Molecular dynamics simulations of hyaluronan have revealed the inherent flexibility of this glycosaminoglycan in solution. Crystal structures of hyaluronan-digesting enzymes have provided the first direct insights into the molecular basis of hyaluronan-protein interactions. Various studies on hyaluronan-binding proteins suggest there is considerable diversity in their mode of interaction with hyaluronan, which might result in many different bound conformations of the polysaccharide.",

author = "Day, {Anthony J.} and Sheehan, {John K.}",

year = "2001",

month = sep,

day = "1",

doi = "10.1016/S0959-440X(00)00256-6",

language = "English",

volume = "11",

pages = "617--622",

journal = "Current Opinion in Structural Biology",

issn = "1879-033X",

publisher = "Elsevier BV",

number = "5",

}

TY - JOUR

T1 - Hyaluronan: Polysaccharide chaos to protein organisation

AU - Day, Anthony J.

AU - Sheehan, John K.

PY - 2001/9/1

Y1 - 2001/9/1

N2 - Molecular dynamics simulations of hyaluronan have revealed the inherent flexibility of this glycosaminoglycan in solution. Crystal structures of hyaluronan-digesting enzymes have provided the first direct insights into the molecular basis of hyaluronan-protein interactions. Various studies on hyaluronan-binding proteins suggest there is considerable diversity in their mode of interaction with hyaluronan, which might result in many different bound conformations of the polysaccharide.

AB - Molecular dynamics simulations of hyaluronan have revealed the inherent flexibility of this glycosaminoglycan in solution. Crystal structures of hyaluronan-digesting enzymes have provided the first direct insights into the molecular basis of hyaluronan-protein interactions. Various studies on hyaluronan-binding proteins suggest there is considerable diversity in their mode of interaction with hyaluronan, which might result in many different bound conformations of the polysaccharide.

U2 - 10.1016/S0959-440X(00)00256-6

DO - 10.1016/S0959-440X(00)00256-6

M3 - Article

C2 - 11785764

SN - 1879-033X

VL - 11

SP - 617

EP - 622

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 5

ER -

Hyaluronan: Polysaccharide chaos to protein organisation

Abstract

Access to Document

Fingerprint

Cite this