Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.

Proteins - 1 Mar 1998

Schindler T, Perl D, Graumann P, Sieber V, Marahiel M A, Schmid F X

Abstract excerpt

In the cold-shock protein CspB from Bacillus subtilis three exposed Phe residues (F15, F17, and F27) are essential for its function in binding to single-stranded nucleic acids. Usually, the hydrophobic Phe side chains are buried in folded proteins. We asked here whether the exposition of the essential Phe residues could be a cause for the very low conformational stability of CspB. Urea-induced and heat-induced...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacillus subtilis
Share to Bacterial Proteins
Share to Carrier Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 9533624
DOI: 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.PMID 9533624Read ↗

T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB.Semantic proximity Read ↗

Key role of coulombic interactions for the folding transition state of the cold shock protein.Semantic proximity Read ↗

Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells.Semantic proximity Read ↗

Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability.Semantic proximity Read ↗

Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions.Semantic proximity Read ↗

The mechanism of nucleic acid melting by a CspA family protein.Semantic proximity Read ↗

Electrostatic stabilization of a thermophilic cold shock protein.Semantic proximity Read ↗

Increasing protein stability by improving beta-turns.Semantic proximity Read ↗

Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Semantic proximity Read ↗

Mutational analysis of the nucleoid-associated protein HBsu of Bacillus subtilis.Semantic proximity Read ↗

Acquisition of double-stranded DNA-binding ability in a hybrid protein between Escherichia coli CspA and the cold shock domain of human YB-1.Semantic proximity Read ↗

Acid-induced formation of molten globule states in the wild type Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase and its three mutated forms: G96A, A183T and G96A/A183T.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.