Studies of the aggregation of RNase Sa

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Studies of the aggregation of RNase Sa. / Khasa, Harshit; Kramer, Ryan; Maddux, Nathan; Hamborg, Mette ; Joshi, Sangeeta B; Volkin, David B; Middaugh, C Russell.

In: Journal of Pharmaceutical Sciences, Vol. 103, No. 2, 02.2014, p. 395-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Khasa, H, Kramer, R, Maddux, N, Hamborg, M, Joshi, SB, Volkin, DB & Middaugh, CR 2014, 'Studies of the aggregation of RNase Sa', Journal of Pharmaceutical Sciences, vol. 103, no. 2, pp. 395-9. https://doi.org/10.1002/jps.23841

APA

Khasa, H., Kramer, R., Maddux, N., Hamborg, M., Joshi, S. B., Volkin, D. B., & Middaugh, C. R. (2014). Studies of the aggregation of RNase Sa. Journal of Pharmaceutical Sciences, 103(2), 395-9. https://doi.org/10.1002/jps.23841

Vancouver

Khasa H, Kramer R, Maddux N, Hamborg M, Joshi SB, Volkin DB et al. Studies of the aggregation of RNase Sa. Journal of Pharmaceutical Sciences. 2014 Feb;103(2):395-9. https://doi.org/10.1002/jps.23841

Author

Khasa, Harshit ; Kramer, Ryan ; Maddux, Nathan ; Hamborg, Mette ; Joshi, Sangeeta B ; Volkin, David B ; Middaugh, C Russell. / Studies of the aggregation of RNase Sa. In: Journal of Pharmaceutical Sciences. 2014 ; Vol. 103, No. 2. pp. 395-9.

Bibtex

@article{6cfb8904c10d442b86e2724cfd99e465,
title = "Studies of the aggregation of RNase Sa",
abstract = "Thirty-eight mutants of RNase Sa (ribonuclease from Streptomyces aureofaciens) were examined for their structure, thermal sensitivity, and tendency to aggregate. Although a biphasic correlation was seen between the effect of temperature on structure and the free energy of transfer changes in many of the mutants, little correlation was seen between the time at which aggregation is initiated or the rate of aggregation and the thermal sensitivity of the mutants. It is hypothesized that the nature of contacts between protein molecules in the associated (aggregated) phase rather than structural changes dominates the aggregation process for these series of mutants.",
author = "Harshit Khasa and Ryan Kramer and Nathan Maddux and Mette Hamborg and Joshi, {Sangeeta B} and Volkin, {David B} and Middaugh, {C Russell}",
note = "{\textcopyright} 2013 Wiley Periodicals, Inc. and the American Pharmacists Association.",
year = "2014",
month = feb,
doi = "10.1002/jps.23841",
language = "English",
volume = "103",
pages = "395--9",
journal = "Journal of Pharmaceutical Sciences",
issn = "0022-3549",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Studies of the aggregation of RNase Sa

AU - Khasa, Harshit

AU - Kramer, Ryan

AU - Maddux, Nathan

AU - Hamborg, Mette

AU - Joshi, Sangeeta B

AU - Volkin, David B

AU - Middaugh, C Russell

N1 - © 2013 Wiley Periodicals, Inc. and the American Pharmacists Association.

PY - 2014/2

Y1 - 2014/2

N2 - Thirty-eight mutants of RNase Sa (ribonuclease from Streptomyces aureofaciens) were examined for their structure, thermal sensitivity, and tendency to aggregate. Although a biphasic correlation was seen between the effect of temperature on structure and the free energy of transfer changes in many of the mutants, little correlation was seen between the time at which aggregation is initiated or the rate of aggregation and the thermal sensitivity of the mutants. It is hypothesized that the nature of contacts between protein molecules in the associated (aggregated) phase rather than structural changes dominates the aggregation process for these series of mutants.

AB - Thirty-eight mutants of RNase Sa (ribonuclease from Streptomyces aureofaciens) were examined for their structure, thermal sensitivity, and tendency to aggregate. Although a biphasic correlation was seen between the effect of temperature on structure and the free energy of transfer changes in many of the mutants, little correlation was seen between the time at which aggregation is initiated or the rate of aggregation and the thermal sensitivity of the mutants. It is hypothesized that the nature of contacts between protein molecules in the associated (aggregated) phase rather than structural changes dominates the aggregation process for these series of mutants.

U2 - 10.1002/jps.23841

DO - 10.1002/jps.23841

M3 - Journal article

C2 - 24382748

VL - 103

SP - 395

EP - 399

JO - Journal of Pharmaceutical Sciences

JF - Journal of Pharmaceutical Sciences

SN - 0022-3549

IS - 2

ER -

ID: 111431498