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

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
102L 1992-09-29T00:00:00+0000 1.74 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
103L 1992-09-29T00:00:00+0000 1.9 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
104L 1992-09-29T00:00:00+0000 2.8 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
107L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
108L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
109L 1992-12-17T00:00:00+0000 1.85 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
110L 1992-12-17T00:00:00+0000 1.7 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
111L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
112L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
113L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Relevant UniProtKB Entries

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