Self-interaction chromatography of proteins on a microfluidic monolith.

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Refolding of proteins from inclusion bodies: rational design and recipes.A novel microfluidics-based method for probing weak protein-protein interactions.Multisyringe Chromatography (MSC): An Effective and Low Cost Tool for Water-Soluble Vitamin Separation

P2860

Q34631469-B267CD1F-2918-4BB3-8D5E-5E230A605891 Q43433220-1C5D6D00-B175-4C15-A315-361BFF4B0CF4 Q58126096-F3FEEA35-0038-4DC6-81B9-64D2E2FBCDB9

P2860

Self-interaction chromatography of proteins on a microfluidic monolith.

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http://www.wikidata.org/entity/Q42003461

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Self-interaction chromatography of proteins on a microfluidic monolith.

@en

Self-interaction chromatography of proteins on a microfluidic monolith.

@nl

type

Item

label

Self-interaction chromatography of proteins on a microfluidic monolith.

@en

Self-interaction chromatography of proteins on a microfluidic monolith.

@nl

prefLabel

Self-interaction chromatography of proteins on a microfluidic monolith.

@en

Self-interaction chromatography of proteins on a microfluidic monolith.

@nl

P1476

Self-interaction chromatography of proteins on a microfluidic monolith.

@en

P2093

Cristina Martin

http://www.w3.org/2001/XMLSchema#string

P2860

Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements.

Enzymatic microreactor-on-a-chip: protein mapping using trypsin immobilized on porous polymer monoliths molded in channels of microfluidic devices.

Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen

Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography

A consistent experimental and modeling approach to light-scattering studies of protein-protein interactions in solution.

Measurements of protein self-association as a guide to crystallization.

Determination of pore size distributions of porous chromatographic adsorbents by inverse size-exclusion chromatography.

Preparation and HPLC applications of rigid macroporous organic polymer monoliths.

Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates.

Patterns of protein protein interactions in salt solutions and implications for protein crystallization.

P304

216-222

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.BEJ.2010.10.016

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Abraham M. Lenhoff

P577

2011-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

49777842

http://www.w3.org/2001/XMLSchema#string

P698

21258647

http://www.w3.org/2001/XMLSchema#string

P921

microfluidics

P932

3022334

http://www.w3.org/2001/XMLSchema#string

Self-interaction chromatography of proteins on a microfluidic monolith.

about

P2860

P2860

Self-interaction chromatography of proteins on a microfluidic monolith.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932