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II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design.

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10099338

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II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design. (English)

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Tsai AM

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van Zanten JH

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Betenbaugh MJ

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publication date

1 August 1998

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Biotechnology and Bioengineering

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volume

59

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3

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281-285

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cites work

I. Study of protein aggregation due to heat denaturation: A structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering.

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https://api.crossref.org/works/10.1002%2F%28SICI%291097-0290%2819980805%2959%3A3%3C281%3A%3AAID-BIT3%3E3.0.CO%3B2-7

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21 January 2018

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10.1002/(SICI)1097-0290(19980805)59:3<281::AID-BIT3>3.0.CO;2-7

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Europe PubMed Central

PubMed publication ID

10099338

retrieved

18 May 2018

reference URL

http://europepmc.org/abstract/MED/10099338

PubMed publication ID

10099338

1 reference

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Europe PubMed Central

PubMed publication ID

10099338

retrieved

18 May 2018

reference URL

http://europepmc.org/abstract/MED/10099338

(Q53696092)

II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design.

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