Structure dynamics of proteins by hydrogen exchange methods

Barksdale, Alfred D.; Knox, D.; Rosenberg, Andreas

doi:10.1016/s0006-3495(80)84994-0

Cited by 3 publications

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“…Equation (6) has been applied to hydrogen-exchange data for ly~ozyme,~ myoglobin, muscle creatine kinase, and, with c = 0, to hemoglobin? Equation (5) may be transformed to provide a dimensionless representation of the pdf4:…”

Section: Gregorymentioning

confidence: 99%

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Comparison of analytically and numerically derived hydrogen exchange‐rate distribution functions

Gregory

1983

Biopolymers

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SynopsisHydrogen exchange-rate probability density functions for lysozyme have been derived by numerical Laplace inversion with the computer program CONTIN. The resulting solution set includes a smooth bimodal solution in agreement with previous analytical results together with a smooth three-peak solution. Numerical analysis of lysozyme hydrogen-exchange data in glycerol/water cosolvent mixtures confirms the previous assignment of the slow-exchange peak to an exchange mechanism involving reversible unfolding. Physicochemical constraints that can reduce the size of the solution set are described. The results are compared with those obtained from previous analytical methods and the limitations of the discrete class and analytical approaches are discussed.

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Section: Gregorymentioning

confidence: 99%

“…However, before discussing this point we should make some comment concerning the imposition on the data of a gamma distribution that is implied by the use of Eqs. (6) and (9).…”

Section: The Power Law Functionmentioning

confidence: 99%

Comparison of analytically and numerically derived hydrogen exchange‐rate distribution functions

Gregory

1983

Biopolymers

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Acquisition and Interpretation of Hydrogen Exchange Data from Peptides, Polymers, and Proteins

Barksdale

Rosenberg

1982

Methods of Biochemical Analysis

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Krishnan

Randolph

et al. 2003

Pharmaceutical Research

1,232

451

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Irreversible protein aggregation is problematic in the biotechnology industry, where aggregation is encountered throughout the lifetime of a therapeutic protein, including during refolding, purification, sterilization, shipping, and storage processes. The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.

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Structure dynamics of proteins by hydrogen exchange methods

Cited by 3 publications

References 2 publications

Comparison of analytically and numerically derived hydrogen exchange‐rate distribution functions

Comparison of analytically and numerically derived hydrogen exchange‐rate distribution functions

Acquisition and Interpretation of Hydrogen Exchange Data from Peptides, Polymers, and Proteins

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