Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7606193 | International Journal of Mass Spectrometry | 2011 | 8 Pages |
Abstract
⺠The all-helical protein, DnaBN, exhibited EX1 type hydrogen exchange at pH 7.2. ⺠The protein was cyclized by joining the N- and C-termini through peptide linkers that were three, four, five or nine amino acids long. ⺠The rate of exchange for the slowly exchanging protons decreased for both the linear and cyclized proteins as linker length increased, correlating with predictions that the C-terminal helix of the protein would be extended by addition of these extra amino acids and stabilizing the protein.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Thitima Urathamakul, Neal K. Williams, Nicholas E. Dixon, Jennifer L. Beck,