iam assigning 95 aminoacid residue protein . i can see 76 cross peaks in hsqc on 700 vnmr cryob . still some peaks are missing . i tried at modified ph conditions , buffer ionic strength and d2o percentage ( 5 to 10 percent ).but no significant improvement
is their any experment to get best number of cross peaks in hsqc ?
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Peak height versus peak volume
Given a standard NOESY-based protein structure determination: Does anyone have any information on the benefits of measuring peak intensity by a volume integration method rather than simply measuring the peak height.
Obviously integration is theoretically more accurate, but does it make any difference to the quality of the structures produced? especially if peak lineshapes are comparable?
I was hoping to find some study comparing structures produced by both methods.....
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Abstract Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding 1H,15N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its...
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
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[Question from NMRWiki Q&A forum] Examples of protein degradation eg HSQC?
Examples of protein degradation eg HSQC?
Anyone know any websites or papers that show protein degradation in an HSQC for example? I wanted to know what to look for in old samples when I have them. Either that, or could someone put one up on the wiki for me to look at?
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