PMID- 34845910
OWN - NLM
STAT- MEDLINE
DCOM- 20220221
LR  - 20220221
IS  - 1520-5207 (Electronic)
IS  - 1520-5207 (Linking)
VI  - 126
IP  - 5
DP  - 2022 Feb 10
TI  - Comparative Analysis of Tryptophan Dynamics in Spectrin and Its Constituent 
      Domains: Insights from Fluorescence.
PG  - 1045-1053
LID - 10.1021/acs.jpcb.1c08600 [doi]
AB  - Spectrin is a cytoskeletal protein ubiquitous in metazoan cells that acts as a 
      liaison between the plasma membrane and the cellular interior and imparts 
      mechanical stability to the plasma membrane. Spectrin is known to be highly 
      dynamic, with an appreciable degree of torsional and segmental mobility. In this 
      context, we have earlier utilized the red edge excitation shift (REES) approach 
      to report the retention of restricted solvation dynamics and local structure in 
      the vicinity of spectrin tryptophans on urea denaturation and loss of spectrin 
      secondary structure. As a natural progression of our earlier work, in this work, 
      we carried out a biophysical dissection of tryptophan solvation and rotational 
      dynamics in spectrin and its constituent domains, in order to trace the origin of 
      local structure retention observed in denatured spectrin. Our results show that 
      the ankyrin binding domain (and, to a lesser extent, the beta-tetramerization 
      domain) is capable of retention of local structure, similar to that observed for 
      intact spectrin. However, all alpha-chain domains studied exhibit negligible 
      retention of local structure on urea denaturation. Such a stark chain-specific 
      retention of local structure could originate from the fact that the beta-chain 
      domains possess specialized functions, where conservation of local (structural) 
      integrity may be a prerequisite for optimum cellular function. To the best of our 
      knowledge, these observations represent one of the first systematic biophysical 
      dissections of spectrin dynamics in terms of its constituent domains and add to 
      emerging literature on comprehensive domain-based analysis of spectrin 
      organization, dynamics, and function.
FAU - Pal, Sreetama
AU  - Pal S
AUID- ORCID: 0000-0002-7153-1402
AD  - CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, 
      India.
FAU - Bose, Dipayan
AU  - Bose D
AD  - Crystallography and Molecular Biology Division, Saha Institute of Nuclear 
      Physics, 1/AF Bidhannagar, Kolkata 700 064, India.
AD  - Homi Bhabha National Institute, Anushaktinagar, Mumbai 400 094, India.
FAU - Chakrabarti, Abhijit
AU  - Chakrabarti A
AD  - Crystallography and Molecular Biology Division, Saha Institute of Nuclear 
      Physics, 1/AF Bidhannagar, Kolkata 700 064, India.
AD  - Homi Bhabha National Institute, Anushaktinagar, Mumbai 400 094, India.
FAU - Chattopadhyay, Amitabha
AU  - Chattopadhyay A
AUID- ORCID: 0000-0002-2618-2565
AD  - CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, 
      India.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20211130
PL  - United States
TA  - J Phys Chem B
JT  - The journal of physical chemistry. B
JID - 101157530
RN  - 0 (Cytoskeletal Proteins)
RN  - 12634-43-4 (Spectrin)
RN  - 8DUH1N11BX (Tryptophan)
SB  - IM
MH  - Animals
MH  - Cytoskeletal Proteins/metabolism
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - *Spectrin/chemistry
MH  - *Tryptophan/chemistry
EDAT- 2021/12/01 06:00
MHDA- 2022/02/22 06:00
CRDT- 2021/11/30 08:42
PHST- 2021/12/01 06:00 [pubmed]
PHST- 2022/02/22 06:00 [medline]
PHST- 2021/11/30 08:42 [entrez]
AID - 10.1021/acs.jpcb.1c08600 [doi]
PST - ppublish
SO  - J Phys Chem B. 2022 Feb 10;126(5):1045-1053. doi: 10.1021/acs.jpcb.1c08600. Epub 
      2021 Nov 30.