Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone-Reference-Cited by-同舟云学术

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Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone

Published:1992-09-15 Issue:36 Volume:31 Page:8587-8596
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Abildgaard Frits,Joergensen Anne Marie Munk,Led Jens J.,Christensen Thorkild,Jensen Ejnar B.,Junker Flemming,Dalboege Henrik

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00151a028

Cited by 24 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Quantitative NMR in Quality Control;Quality Control of Chinese Medicines;2024

2. Insight into the Microcosm of the Human Growth Hormone and Its Interactions with Polymers and Copolymers: A Molecular Dynamics Perspective;Langmuir;2020-12-23

3. An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes;Nanoscale Advances;2020

4. Development of a Transnasal Delivery System for Recombinant Human Growth Hormone (rhGH): Effects of the Concentration and Molecular Weight of Poly-L-arginine on the Nasal Absorption of rhGH in Rats;Biological & Pharmaceutical Bulletin;2016

5. Specific and Nonspecific Interactions in Ultraweak Protein–Protein Associations Revealed by Solvent Paramagnetic Relaxation Enhancements;Journal of the American Chemical Society;2014-07-10

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