From owner-biophys@hgmp.mrc.ac.uk Wed Sep 18 18:45:13 2002 Return-Path: Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with SMTP id BF62E17BA2 for ; Wed, 18 Sep 2002 18:45:12 +0100 (BST) Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 7BF7717BB7 for ; Wed, 18 Sep 2002 18:45:11 +0100 (BST) Received: from niobium.hgmp.mrc.ac.uk (niobium [193.62.192.41]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id BDBD617BA2 for ; Wed, 18 Sep 2002 18:45:09 +0100 (BST) Received: (from news@localhost) by niobium.hgmp.mrc.ac.uk (8.9.3+Sun/8.8.8) id SAA14087 for biophys-list@hgmp.mrc.ac.uk; Wed, 18 Sep 2002 18:45:09 +0100 (BST) X-Authentication-Warning: niobium.hgmp.mrc.ac.uk: news set sender to using -f From: saco@moon.yerphi.am (Saco) X-Newsgroups: bionet.biophysics Subject: Re: Ends of sequence critical to tertiary structure too? Date: 18 Sep 2002 10:45:06 -0700 Organization: http://groups.google.com/ Lines: 15 Message-ID: <85160b48.0209180945.389b152@posting.google.com> References: Content-Type: text/plain; charset=ISO-8859-1 Content-Transfer-Encoding: 8bit X-Complaints-To: groups-abuse@google.com To: biophys@hgmp.mrc.ac.uk X-Razor-id: 41d2f57abccc181dcbd9ddfd02e4958ba61fe091 Sender: owner-biophys@hgmp.mrc.ac.uk Precedence: bulk "Adrian" wrote in message news:... > You know amino acid sequence probably totally determines into what tertiary > structure the protein folds. Besides amino acid sequence, environment (pH level, temperature, etc.) dictates tertiary structure too. > The question: are the amino acids postioned near very ends of sequences also > so critical for the process of folding? What will it happen if a sequence is > slightly shortened by removing 1 or 2 aminoacids from sequence's ends? (Or > if very end is altered by exchanging an aminoacid?) Will the tertiary > structure change significantly? My guess is that the longer the sequence, the less important are end group effects, but there might be special cases though. .