Knitting and snipping: chaperones in β-helix folding

Eike C Schulz; Ralf Ficner

doi:10.1016/j.sbi.2011.01.009

Knitting and snipping

Standard

Knitting and snipping : chaperones in β-helix folding. / Schulz, Eike C; Ficner, Ralf.

In: CURR OPIN STRUC BIOL, Vol. 21, No. 2, 04.2011, p. 232-9.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Schulz, EC & Ficner, R 2011, 'Knitting and snipping: chaperones in β-helix folding', CURR OPIN STRUC BIOL, vol. 21, no. 2, pp. 232-9. https://doi.org/10.1016/j.sbi.2011.01.009

APA

Schulz, E. C., & Ficner, R. (2011). Knitting and snipping: chaperones in β-helix folding. CURR OPIN STRUC BIOL, 21(2), 232-9. https://doi.org/10.1016/j.sbi.2011.01.009

Vancouver

Schulz EC, Ficner R. Knitting and snipping: chaperones in β-helix folding. CURR OPIN STRUC BIOL. 2011 Apr;21(2):232-9. https://doi.org/10.1016/j.sbi.2011.01.009

Bibtex

@article{faf5165676d34b69910e874d2749bf07,

title = "Knitting and snipping: chaperones in β-helix folding",

abstract = "Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.",

keywords = "Molecular Chaperones/chemistry, Protein Folding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary",

author = "Schulz, {Eike C} and Ralf Ficner",

year = "2011",

month = apr,

doi = "10.1016/j.sbi.2011.01.009",

language = "English",

volume = "21",

pages = "232--9",

journal = "CURR OPIN STRUC BIOL",

issn = "0959-440X",

publisher = "Elsevier Limited",

number = "2",

}

RIS

TY - JOUR

T1 - Knitting and snipping

T2 - chaperones in β-helix folding

AU - Schulz, Eike C

AU - Ficner, Ralf

PY - 2011/4

Y1 - 2011/4

N2 - Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.

AB - Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.

KW - Molecular Chaperones/chemistry

KW - Protein Folding

KW - Protein Multimerization

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

U2 - 10.1016/j.sbi.2011.01.009

DO - 10.1016/j.sbi.2011.01.009

M3 - SCORING: Review article

C2 - 21330133

VL - 21

SP - 232

EP - 239

JO - CURR OPIN STRUC BIOL

JF - CURR OPIN STRUC BIOL

SN - 0959-440X

IS - 2

ER -