title: Utility of computational structural biology in mass spectrometry.
abstract: Recent developments of mass spectrometry (MS) allow us to identify, estimate, and characterize proteins and protein complexes. At the same time, structural biology helps to determine the protein structure and its structure-function relationship. Together, they aid to understand the protein structure, property, function, protein-complex assembly, protein-protein interaction and dynamics. The present chapter is organized with illustrative results to demonstrate how experimental mass spectrometry can be combined with computational structural biology for detailed studies of protein's structures. We have used tumor differentiation factor protein/peptide as ligand and Hsp70/Hsp90 as receptor protein as examples to study ligand-protein interaction. To investigate possible protein conformation we will describe two proteins, lysozyme and myoglobin.
authors: Department of Chemistry & Biomolecular Science, Biochemistry & Proteomics Group, Structural Biology & Molecular Modeling Unit, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, 13699-5810, USA.
authors: Urmi
authors: U
authors: Roy
authors: Alisa G
authors: AG
authors: Woods
authors: Izabela
authors: I
authors: Sokolowska
authors: Costel C
authors: CC
authors: Darie
mesh_terms: D000818:Animals; D019295:Computational Biology / Q000379:methods*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D009113:Muramidase / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D009211:Myoglobin; D009363:Neoplasm Proteins; D009113:Muramidase