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Mutations and protein stability.

Abstract

Study holds ProTherm entries: 1220, 1221, 1222, 1223, 1224, 1225, 1226, 1227 Extra Details: point mutations; T4 lysozyme; protein structure;,protein stability

Submission Details

ID: FcySJ4yo3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:16 p.m.

Version: 1

Publication Details

Schellman JA;Lindorfer M;Hawkes R;Grutter M,Biopolymers (1981) Mutations and protein stability. PMID:7306671

Additional Information

Study Summary

Number of data points	27
Proteins	Endolysin ; Endolysin ; Endolysin
Unique complexes	7
Assays/Quantities/Protocols	Experimental Assay: dCp pH:3.0 ; Experimental Assay: Tm pH:3.0 ; Experimental Assay: activity ; Experimental Assay: dCp pH:2.0 ; Experimental Assay: Tm pH:2.0 ; Derived Quantity: dTm pH:3.0 ; Derived Quantity: dTm pH:2.0
Libraries	Mutations for sequence MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

Structure view and single mutant data analysis

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Study data

Colors:	D	E	R	H	K	S	T	N	Q	A	V	I	L	M	F	Y	W	C	G	P

Data Distribution

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Relevant PDB Entries

Structure ID	Release Date	Resolution	Structure Title

Relevant UniProtKB Entries

Percent Identity	Matching Chains	Protein	Accession	Entry Name
100.0		Endolysin	P00720	ENLYS_BPT4