1c:{"metadata":[["$","title","0",{"children":"NIH VideoCast - Seeing the Invisible by Solution NMR Spectroscopy"}],["$","meta","1",{"name":"description","content":"Many biochemical processes proceed through the formation of functionally important intermediates. For example, ligand binding, enzyme catalysis and protein folding may all involve the formation of one or more intermediates along the reaction coordinate connecting the initial and final protein states. A complete understanding of each process requires, therefore, characterization of these intermediates in detail. While methods exist for studying the endpoints of these processes at atomic resolution in many cases, similar studies of the intermediates remain elusive. NMR methods for seeing such ‘invisible’ states will be described, along with a number of applications to protein folding illustrating the power of the methodology.\n

\nhttp://abragam.med.utoronto.ca/Kay.html\n
\n
\nNIH Director's Wednesday Afternoon Lecture Series
"}],["$","meta","2",{"name":"publisher","content":"National Institutes of Health"}],["$","meta","3",{"property":"og:title","content":"NIH VideoCast - Seeing the Invisible by Solution NMR Spectroscopy"}],["$","meta","4",{"property":"og:description","content":"Many biochemical processes proceed through the formation of functionally important intermediates. For example, ligand binding, enzyme catalysis and protein folding may all involve the formation of one or more intermediates along the reaction coordinate connecting the initial and final protein states. A complete understanding of each process requires, therefore, characterization of these intermediates in detail. While methods exist for studying the endpoints of these processes at atomic resolution in many cases, similar studies of the intermediates remain elusive. NMR methods for seeing such ‘invisible’ states will be described, along with a number of applications to protein folding illustrating the power of the methodology.\n

\nhttp://abragam.med.utoronto.ca/Kay.html\n
\n
\nNIH Director's Wednesday Afternoon Lecture Series
"}],["$","meta","5",{"property":"og:url","content":"https://uat.d1rkikwu4q8tg.amplifyapp.com/watch/996d491b-d5db-11f0-9cf9-12c45c580ad9"}],["$","meta","6",{"property":"og:site_name","content":"NIH VideoCast"}],["$","meta","7",{"property":"og:image","content":"https://nihcit.rev.vbrick.com/api/v2/media/videos/thumbnails/139fb112-aa61-44d0-96d6-e8485467523d.jpg"}],["$","meta","8",{"property":"og:type","content":"website"}],["$","meta","9",{"name":"twitter:card","content":"summary_large_image"}],["$","meta","10",{"name":"twitter:title","content":"NIH VideoCast - Seeing the Invisible by Solution NMR Spectroscopy"}],["$","meta","11",{"name":"twitter:description","content":"Many biochemical processes proceed through the formation of functionally important intermediates. For example, ligand binding, enzyme catalysis and protein folding may all involve the formation of one or more intermediates along the reaction coordinate connecting the initial and final protein states. A complete understanding of each process requires, therefore, characterization of these intermediates in detail. While methods exist for studying the endpoints of these processes at atomic resolution in many cases, similar studies of the intermediates remain elusive. NMR methods for seeing such ‘invisible’ states will be described, along with a number of applications to protein folding illustrating the power of the methodology.\n

\nhttp://abragam.med.utoronto.ca/Kay.html\n
\n
\nNIH Director's Wednesday Afternoon Lecture Series
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