Studies of the aggregation of RNase Sa

Harshit Khasa; Ryan Kramer; Nathan Maddux; Mette  Hamborg; Sangeeta B Joshi; David B Volkin; C Russell Middaugh

doi:10.1002/jps.23841

Studies of the aggregation of RNase Sa

Harshit Khasa, Ryan Kramer, Nathan Maddux, Mette Hamborg, Sangeeta B Joshi, David B Volkin, C Russell Middaugh

Centre for Medical Parasitology

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.

Originalsprog	Engelsk
Tidsskrift	Journal of Pharmaceutical Sciences
Vol/bind	103
Udgave nummer	2
Sider (fra-til)	395-9
Antal sider	5
DOI	https://doi.org/10.1002/jps.23841
Status	Udgivet - feb. 2014

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10.1002/jps.23841

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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.",

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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

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

SN - 0022-3549

VL - 103

SP - 395

EP - 399

JO - Journal of Pharmaceutical Sciences

JF - Journal of Pharmaceutical Sciences

IS - 2

ER -

Studies of the aggregation of RNase Sa

Abstract

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