June 9, 2001Biochemistry

Mapping Protein Interfaces with a Fluorogenic Cross-Linker and Mass Spectrometry: Application to Nebulin−Calmodulin Complexes

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Population

Nebulin-calmodulin complexes (CaM and ND66, a four-module cloned fragment from the C-terminus of nebulin)

Design

Preclinical

Authors

ASAndrea SinzLuther University KWKuan WangXinjiang Medical University

Discussion

Member takes

Implication

Suggests possible CaM-actin competition on nebulin; leaves open functional consequences for sarcomere regulation.

Structured PICO

Population

Nebulin-calmodulin complexes (CaM and ND66, a four-module cloned fragment from the C-terminus of nebulin)

Intervention

Two-stage cross-linking with 2-iminothiolane and dibromobimane followed by in-gel chymotryptic digestion, HPLC with fluorescence detection, and mass spectrometry (ESI-MS/MS)

Outcome

Identification of inter- and intramolecular cross-linking sites to define molecular interfaces and patterns of protein folding

Mapping of the nebulin-calmodulin interface suggests proximity to the nebulin-actin interface, indicating potential competition for binding on the thin filaments of the skeletal muscle sarcomere.

Cite This Study

Sinz et al. (2001) studied this question.

synapsesocial.com/papers/6a871a38d00295e3b4bf015e https://doi.org/10.1021/bi010259+

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Ask AI

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Mapping Protein Interfaces with a Fluorogenic Cross-Linker and Mass Spectrometry: Application to Nebulin−Calmodulin Complexes

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Mapping Protein Interfaces with a Fluorogenic Cross-Linker and Mass Spectrometry: Application to Nebulin−Calmodulin Complexes

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider