Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.

about

Protein stabilization by tuning the steric restraint at the reverse turn† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc05163h.

P2860

Q55063580-D6E0D9B0-0A99-45CB-AE34-58A8002357AF

P2860

Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.

Item

http://www.wikidata.org/entity/Q46427708

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@en

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@nl

type

Item

label

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@en

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@nl

prefLabel

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@en

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@nl

P1476

Using Cooperatively Folded Pep ...... d Conformational Propensities.

@en

P2093

Evan T Powers

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

P2860

Structure-function-folding relationship in a WW domain

Evaluating beta-turn mimics as beta-sheet folding nucleators

Carbohydrate-Aromatic Interactions in Proteins

NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1

Structural and Energetic Basis of Carbohydrate–Aromatic Packing Interactions in Proteins

Some factors in the interpretation of protein denaturation

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.

Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards.

The helical s constant for alanine in water derived from template-nucleated helices.

P304

1875-1882

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

P31

scholarly article

P356

10.1021/ACS.ACCOUNTS.7B00195

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

P407

English

P433

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

P478

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

P50

Maziar S Ardejani

Jeffery W. Kelly

P577

2017-07-19T00:00:00Z

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

P698

28723063

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

P932

5584629

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

Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.

about

P2860

P2860

Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932