TY - CHAP
T1 - NMR Studies of Protein-Glycosaminoglycan Interactions
AU - Wang, Xu
N1 - Publisher Copyright:
© The Royal Society of Chemistry 2017.
PY - 2017
Y1 - 2017
N2 - Glycosaminoglycans (GAGs) are a class of linear, sulfated polysaccharides. These extracellular polysaccharides interact with a range of protein partners and are active in controlling important biological phenomena, including reproduction, cell growth and differentiation, blood coagulation and immune system activation. As a result, interests in developing methods to control specific protein-GAG interactions are high. However, little high-resolution structural information on protein-GAG interactions is available, and predicting a protein's specificity for different GAG motifs remains challenging. Solution NMR has played crucial roles in analyzing specificity and dynamics of protein-GAG interactions. It is instrumental in determining GAG-binding sites of proteins and elucidating GAG-induced changes in protein dynamics. NMR's adaptability to GAG size and sulfation density means the technique can be used to investigate a large class of protein-GAG interactions even if homogeneous GAG samples are not available. In this chapter we will review some of the popular NMR techniques for studying protein-GAG interactions will be reviewed. Challenges in the study of protein-GAG systems and new techniques that may help in overcoming these challenges will also be examined.
AB - Glycosaminoglycans (GAGs) are a class of linear, sulfated polysaccharides. These extracellular polysaccharides interact with a range of protein partners and are active in controlling important biological phenomena, including reproduction, cell growth and differentiation, blood coagulation and immune system activation. As a result, interests in developing methods to control specific protein-GAG interactions are high. However, little high-resolution structural information on protein-GAG interactions is available, and predicting a protein's specificity for different GAG motifs remains challenging. Solution NMR has played crucial roles in analyzing specificity and dynamics of protein-GAG interactions. It is instrumental in determining GAG-binding sites of proteins and elucidating GAG-induced changes in protein dynamics. NMR's adaptability to GAG size and sulfation density means the technique can be used to investigate a large class of protein-GAG interactions even if homogeneous GAG samples are not available. In this chapter we will review some of the popular NMR techniques for studying protein-GAG interactions will be reviewed. Challenges in the study of protein-GAG systems and new techniques that may help in overcoming these challenges will also be examined.
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U2 - 10.1039/9781782623946-00250
DO - 10.1039/9781782623946-00250
M3 - Chapter
AN - SCOPUS:85020484409
T3 - New Developments in NMR
SP - 250
EP - 268
BT - Biophysics and Biochemistry of Cartilage by NMR and MRI
A2 - Price, William S.
A2 - Kato, Koichi
A2 - Peters, Thomas
PB - Royal Society of Chemistry
ER -